JP2009022248A - Enzyme network and enzyme fuel cell - Google Patents

Abstract

<P>PROBLEM TO BE SOLVED: To provide a means more efficiently generating electric energy. <P>SOLUTION: Enzyme network 100 is provided with a first enzyme network comprising a plurality of enzymes catalyzing a series of chemical reactions in which D-glucose is metabolized to 6-phospho-D-gluconate and a second enzyme network comprising an enzyme of ID[4.2.1.12], an enzyme of ID[4.1.2.14] and a plurality of enzymes catalyzing a series of chemical reactions in which pyruvate and (2R)-2-hydroxy-3-(phosphonoxy)-propanal are metabolized to CO<SB>2</SB>. The present invention is, for instance, applicable to a biofuel cell. <P>COPYRIGHT: (C)2009,JPO&INPIT

Description

  The present invention relates to an enzyme network and an enzyme fuel cell, and more particularly to an enzyme network and an enzyme fuel cell that can generate electric energy more efficiently.

  In recent years, attention to environmental problems has increased, and the utilization of biotechnology has been studied in various technical fields as part of the solution. Along with this, research on biotechnology has been actively conducted.

  For example, there is a biofuel cell that uses, as a power source, energy obtained in the process of decomposing a high energy compound such as glucose into carbon dioxide using an enzyme (see, for example, Non-Patent Document 1). The production of metabolites using such enzyme reactions can be used in various fields such as medicine and chemistry.

  In the usual case, enzymes have reaction specificity and catalyze only certain chemical reactions. Therefore, in the production of metabolites by such an enzyme reaction, a plurality of enzymes are usually used in combination. In other words, the exhausted substance that is the target substance is generated from the starting material that is the material through a plurality of types of chemical reactions by a plurality of types of enzymes. This chemical reaction pathway is called a metabolic pathway. At present, thousands of kinds of enzymes are known, and each catalyzes a chemical reaction, so that a variety of metabolic pathway networks are constructed in the whole enzyme.

  When producing an effluent from a starting material, a necessary one is selected from those enzyme groups, and a metabolic pathway connecting the starting material and the effluent is constructed. The selection of the pathway, that is, the selected enzyme Changes the efficiency of the chemical reaction (metabolism). In other words, the productivity of emitted substances changes.

Korneel Rabaey and Willy Verstraete, Microbial fuel cells: novel biotechnology for energy generation, TRENDS in Biotechnology Vol.23 No.6, ScienceDirect, June 2005, P291-298

  However, conventionally, a biofuel cell (enzyme fuel cell) has been constructed using living E. coli as an enzyme group, the metabolic pathway itself is complicated, and a reaction in the reverse direction is caused rather than the forward direction. Since an easy enzyme is contained, there is a fear that electric energy cannot be efficiently generated.

  The present invention has been proposed in view of such a conventional situation, and enables electric energy to be generated more efficiently.

  A first aspect of the present invention is an enzyme network consisting of a plurality of enzymes that catalyzes a series of chemical reactions for metabolizing glucose (D-Glucose) to carbon dioxide (CO2), wherein D-Glucose is converted to 6-Phospho. A first enzyme network composed of a plurality of enzymes that catalyze a series of chemical reactions to be metabolized to -D-gluconate; and 6-Phospho-D-gluconate produced by catalysis of the first enzyme network, Dehydro-3-deoxy-6-phospho-D-gluconate and phosphogluconate dehydratase (EC number 4.2.1.12) catalyzing the chemical reaction metabolized to H2O, and the phosphogluconate dehydratase (EC number 4.2.1.12) catalyzed and produced 2-dehydro-3-deoxy-6-phospho-D-gluconate catalyzes a chemical reaction that metabolizes Pyruvate to (2R) -2-Hydroxy-3- (phosphonooxy) -propanal Catalyzed by -phosphogluconate aldolase (EC number 4.1.2.14) and 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14) A series of chemical reactions to be metabolized to CO2 the generated Pyruvate and (2R) -2-Hydroxy-3- (phosphonooxy) -propanal an enzyme network and a second enzyme network of enzymes that catalyze.

  The second enzyme network is (2R) -2-Hydroxy-3- (phosphonooxy) -propanal, NADP + produced by catalyzing the 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14). And glyceraldehyde-3-phosphate dehydrogenase (EC number 1.2.1.9) that catalyzes a chemical reaction that metabolizes H2O to 3-Phospho-D-glycerate, NADPH, h, and h.

  The second enzyme network includes a plurality of (2R) -2-Hydroxy-3- (phosphonooxy) -propanal produced by catalyzing the 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14). A third enzyme network comprising a plurality of enzymes that catalyze a series of chemical reactions that can be metabolized to CO2 and also to pyruvate.

  The third enzyme network is (2R) -2-Hydroxy-3- (phosphonooxy) -propanal, NADP + produced by catalyzing the 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14). And glyceraldehyde-3-phosphate dehydrogenase (EC number 1.2.1.9) that catalyzes a chemical reaction that metabolizes H2O to 3-Phospho-D-glycerate, NADPH, h, and h, and the glyceraldehyde-3-phosphate dehydrogenase ( 3-phosphoglycerate phosphatase (EC number 3.1.3.38) that catalyzes a chemical reaction that metabolizes 3-Phospho-D-glycerate and H2O catalyzed to EC number 1.2.1.9) to D-Glycerate and Orthophosphate, Hydroxypyruvate reductase (EC number 1.1.1.81) that catalyzes a chemical reaction that metabolizes D-Glycerate and NADP + produced by catalyzing the 3-phosphoglycerate phosphatase (EC number 3.1.3.38) to Hydroxypyruvate, NADPH, and h; Hydrox produced by catalyzing the hydroxypyruvate reductase (EC No. 1.1.1.81) hydroxypyruvate decarboxylase (EC number 4.1.1.40) that catalyzes a chemical reaction that metabolizes ypyruvate to Glycolaldehyde and CO2, and Glycolaldehyde, NAD +, and H2O produced by catalyzing the hydroxypyruvate decarboxylase (EC number 4.1.1.40), Glycolate, NADH, h, and glycolaldehyde dehydrogenase (EC number 1.2.1.21) that catalyzes a chemical reaction metabolized to h, and Glycolate and Acceptor produced by catalyzing the glycolaldehyde dehydrogenase (EC number 1.2.1.21) And glycolate dehydrogenase (EC number 1.1.99.14) that catalyzes a chemical reaction metabolized to reduced acceptor, and Glyoxylate, Acetyl-CoA, and H2O produced by catalyzing the glycolate dehydrogenase (EC number 1.1.99.14) ( Malate synthase (EC number 2.3.3.9) catalyzing the chemical reaction metabolized to S) -Malate and CoA, and (S) -Malate and NADP + produced by catalyzing the malate synthase (EC number 2.3.3.9) It may include Pyruvate, CO2, and catalyzes a chemical reaction that is metabolized to NADPH malate Dehydrogenase and (EC No. 1.1.1.40).

  The third enzyme network converts Pyruvate, CoA, and NADP + produced by catalysis of the 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14) into Acetyl-CoA, CO2, and NADPH. Further, pyruvate dehydrogenase (EC number 1.2.1.51) that catalyzes a chemical reaction to be metabolized may be included.

  The third enzyme network is a chemical reaction that metabolizes 3-Phospho-D-glycerate produced by catalyzing the glyceraldehyde-3-phosphate dehydrogenase (EC number 1.2.1.9) to 2-Phospho-D-glycerate. Catalyzing the chemical reaction of metabolizing phosphoglycerate mutase (EC No. 5.4.2.1) catalyzing the above and 2-Phospho-D-glycerate produced by catalyzing the phosphoglycerate mutase (EC No. 5.4.2.1) into Phosphoenolpyruvate and H2O Phosphopyruvate hydratase (EC No. 4.2.1.11) and pyruvate kinase (EC No.) that catalyzes the chemical reaction of metabolizing Phosphoenolpyruvate and ADP catalyzed by the phosphopyruvate hydratase (EC No. 4.2.1.11) to ATP and Pyruvate 2.7.1.40) can be further included.

  According to a second aspect of the present invention, there is provided an enzyme fuel cell that uses the catalytic action of an enzyme to metabolize glucose (D-Glucose) into carbon dioxide (CO2) to generate electricity, and the glucose (D-Glucose) ) As a network of enzymes that catalyze a series of chemical reactions that metabolize carbon dioxide (CO2) to the carbon dioxide (CO2), and catalyze a series of chemical reactions that metabolize D-Glucose to 6-Phospho-D-gluconate. 1 enzyme network and chemical reaction to metabolize 6-Phospho-D-gluconate produced by catalysis of the first enzyme network into 2-Dehydro-3-deoxy-6-phospho-D-gluconate and H2O Phosphogluconate dehydratase (EC number 4.2.1.12) that catalyzes the above, and 2-Dehydro-3-deoxy-6-phospho-D-gluconate produced by catalyzing the phosphogluconate dehydratase (EC number 4.2.1.12), and Pyruvate 2-dehydro-3-deo that catalyzes a chemical reaction metabolized to (2R) -2-Hydroxy-3- (phosphonooxy) -propanal xy-phosphogluconate aldolase (EC number 4.1.2.14), Pyruvate produced by catalyzing the 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14) and (2R) -2-Hydroxy-3- An enzyme fuel cell comprising a second enzyme network that metabolizes (phosphonooxy) -propanal to CO2.

  In the first aspect of the present invention, a first enzyme network comprising a plurality of enzymes that catalyze a series of chemical reactions for metabolizing D-Glucose to 6-Phospho-D-gluconate, and the first enzyme network catalyzed Phosphogluconate dehydratase (EC number 4.2.1.12) that catalyzes a chemical reaction that metabolizes the produced 6-Phospho-D-gluconate to 2-Dehydro-3-deoxy-6-phospho-D-gluconate and H2O, 2-Dehydro-3-deoxy-6-phospho-D-gluconate catalyzed by phosphogluconate dehydratase (EC No. 4.2.1.12) was converted to Pyruvate and (2R) -2-Hydroxy-3- (phosphonooxy) -propanal Produced by catalyzing 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14) and 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14), which catalyze the chemical reaction metabolized to A second enzyme net consisting of multiple enzymes that catalyze a series of chemical reactions that metabolize Pyruvate and (2R) -2-Hydroxy-3- (phosphonooxy) -propanal to CO2. Over click and is configured.

  In the second aspect of the present invention, as an enzyme network consisting of a plurality of enzymes that catalyzes a series of chemical reactions that metabolize glucose (D-Glucose) to carbon dioxide (CO2), D-Glucose is 6-Phospho- A first enzyme network that catalyzes a series of chemical reactions that are metabolized to D-gluconate, and 6-Phospho-D-gluconate produced by catalyzing the first enzyme network is converted into 2-Dehydro-3-deoxy-6 -phospho-D-gluconate and phosphogluconate dehydratase (EC number 4.2.1.12) catalyzing the chemical reaction metabolized to H2O and 2-Dehydro-3-deoxy produced by catalyzing phosphogluconate dehydratase (EC number 4.2.1.12) 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.) Catalyzing the chemical reaction of metabolizing -6-phospho-D-gluconate to Pyruvate and (2R) -2-Hydroxy-3- (phosphonooxy) -propanal 2.14), Pyruvate produced by catalyzing 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14) and (2R ) -2-Hydroxy-3- (phosphonooxy) -propanal is provided with a second enzyme network that metabolizes it to CO2.

  According to the present invention, electrical energy can be generated. In particular, electric energy can be generated more efficiently.

  FIG. 1 is a diagram showing a configuration example of an enzyme network to which the present invention is applied.

The enzyme network 100 shown in FIG. 1 comprises a plurality of enzymes that catalyze a series of chemical reactions that metabolize glucose (D-Glucose) to carbon dioxide (CO ₂ ), with glucose as the starting material and CO _{2 as} the emission material. This is a system that forms a metabolic network (metabolic pathway network) that efficiently metabolizes glucose to CO ₂ and discharges it. In addition, the enzyme network 100 emits electrons in the course of its metabolism. That is, the enzyme network 100 is a system that efficiently generates electrical energy from glucose. Therefore, the enzyme network 100 is used as an enzyme network for a biofuel cell (enzyme fuel cell) that generates electricity by metabolizing glucose (D-Glucose) to carbon dioxide (CO ₂ ) by utilizing the catalytic action of the enzyme. It is suitable for.

  First, an outline of the configuration of the enzyme network 100 in FIG. 1 will be described. In FIG. 1, the metabolic pathway of the enzyme network 100 is indicated by arrows (edges). Nodes connected by the edges and indicated by squares in the figure indicate substrates, enzymes, and the like. That is, in FIG. 1, the enzyme network 100 is shown as a series of chemical reactions (enzyme reactions) catalyzed by each enzyme. Specifically, one enzyme reaction is basically shown as the following formula (1), and the enzyme network 100 has a configuration in which a plurality of formulas (1) are linked to each other.

  S → (E + S) → (E + P) → P (1)

  In the formula (1), S represents a substrate, E represents an enzyme, and P represents a product. That is, each process of one enzyme reaction is shown by three edges (four nodes). However, in FIG. 1, common substances such as coenzymes and the like are included in the substrates and products. Further, as shown in FIG. 1, the direction of the arrow (edge) may be reversed. In FIG. 1, for example, nodes indicated by white squares such as the node 111 and the node 114 indicate the terms S and P in the formula (1), for example, gray squares such as the node 112 and the node 113. The nodes shown indicate the terms (E + S) and (E + P) in equation (1). That is, as shown in FIG. 1, the enzyme network 100 is a combination of enzyme reactions having a common substrate and product.

  The simulation results of the enzyme network 100 of FIG. 1 are shown in FIGS. The configuration of the enzyme network 100 will be described more specifically with reference to these.

  The list described in the range 201 in FIG. 2 is a list of enzyme reactions performed in the enzyme network 100, and each row indicates a portion of (E + S) → (E + P) in the equation (1). . For example, “2.7.1.2 [ATP, D-Glucose] → 2.7.1.2 [ADP, D-Glucose 60 phosphate]” in the second line from the top indicates a chemical reaction from node 112 to node 113 in FIG. . These details are described in FIGS. 3 to 10 and will be described later with reference to them.

  In a range 202 of FIG. 2, the final product (exhaust substance) and its concentration (exhaust amount) are shown.

  3 to 10 show the details of the enzyme reaction. Since the configurations of the ranges 211 to 236 in FIGS. 3 to 10 are basically the same, first, the configuration will be described with reference to the range 211 in FIG.

  The ID of the enzyme is shown in “ID” on the first line from the top. This ID is identification information for identifying each enzyme, and is a so-called EC number. The EC number is an ID assigned by the Enzyme Committee of the International Biochemical Union, and consists of a combination of four numbers. Enzymes are classified according to differences in reaction specificity and substrate specificity. The EC number indicates where the enzyme belongs in this category. Of the four numbers, they are subdivided from left to right. The enzyme is further given a system name in which the name of the substrate molecule and the name of the reaction are linked. For some enzymes, common names that are shortened by omitting part of the substrate may be used. In the present embodiment, basically, an EC number is used to identify an enzyme.

  The “Reaction” in the second line from the top shows the enzyme reaction formula. This is the same as the list described in the range 201 of FIG. 2, and shows the part of (E + S) → (E + P) in the equation (1). The description of each range from the range 211 to the range 236 describes the information in units of reaction. Since some enzymes may react in the opposite direction, there may be two reactions for one enzyme. In that case, each reaction is described using two ranges.

“Michaelis Constant” on the third line from the top indicates the Michaelis constant of this enzymatic reaction. The Michaelis constant is a constant used in a reaction rate equation (Michaelis-Menten equation) representing a reaction rate of a chemical reaction. Michaelis constant K _m is the rate k _{+1 at} which enzyme E and substrate S become intermediate complex ES, the rate k ₋₁ at which intermediate complex ES becomes enzyme E and substrate S, and intermediate complex ES as products P and It can be expressed as the following formula (2) by using the speed k ₊₂ to become the enzyme E.

K _m = (k ₋₁ + k ₊₂ ) / k ₊₁ (2)

  If the substrate concentration is S, the Michaelis-Menten equation can be expressed as the following equation (3).

v = (V × [S]) / (K _m + [S]) (3)

  The Michaelis constants of known enzymatic reactions are basically known and are defined, for example, in the database Brenda at the University of Cologne, Germany.

  “Turnover Number” on the fourth line from the top indicates the turnover number of this enzyme reaction. The turnover number indicates the number of substrates reacted per second per enzyme (number of turnover molecules per second per molecule of enzyme). This turnover number is also defined in Brenda, for example, like the Michaelis constant.

  “Specific Activity” on the fifth line from the top indicates the specific activity of this enzyme reaction. Intrinsic activity is essentially the same as the number of turnovers, but in different units. This unique activity is also defined in, for example, Brenda, like the turnover number and Michaelis constant.

  “Organism” on the 6th line from the top is a list of organism names where the enzyme exists in nature. “Amount” in the second line from the bottom indicates the allocated amount (concentration) of the enzyme. “Traffic” in the first line from the bottom indicates the reaction concentration of the enzyme reaction. This reaction rate is a value calculated based on the Michaelis constant, the turnover number, the substrate concentration, the allocated amount of the enzyme, and the like. In other words, the simulation results described below are basically the results of calculations performed using the values registered in Brenda described above. Similarly, any simulator can be used as long as it is a simulator performed using the Michaelis-Menten equation. Even if is used, the simulation result does not change greatly.

  Details of the configuration of the enzyme network 100 of FIG. 1 will be described with reference to the ranges 211 to 236 in which information is described in the above configuration.

  In FIG. 1, a node 111 is “D-Glucose” which is a starting material and is a substrate of an enzyme reaction from the node 112 to the node 113. In the simulation, the concentration of the starting material is set to “40000.0 nmol”. That is, the concentration of each enzyme described below is the concentration when the concentration of the starting material is “40000.0 nmol”. Of course, an arbitrary value can be applied to the concentration of the starting material, but the concentration value of each enzyme needs to be a value corresponding to the concentration of the starting material.

  Information about the enzymatic reaction from node 112 to node 113 is described in range 211 of FIG. That is, the node 112 indicates the enzyme (glucokinase) with the ID “2.7.1.2” and the substrates “D-Glucose” and “ATP” of the enzyme reaction, and the node 113 has the ID “2.7.1.2”. An enzyme (glucokinase) and “ADP” and “D-Glucose 6-phosphate” which are products of this enzyme reaction are shown. The Michaelis constant of this enzymatic reaction is “0.028 mmol / l”, the turnover number is “410.0 / s”, and the specific activity is “370.0 umol / min / mg”. This enzyme (2.7.1.2) can be collected from, for example, E. coli, bacteria, rats, and humans. Further, the allocated amount (concentration) of the enzyme (2.7.1.2) is “6.344967267689803 nmol”. The traffic of this enzymatic reaction was “40000.0 nmol”.

  The node 114 indicates “D-Glucose 6-phosphate”, which is a product of the enzyme reaction from the node 112 to the node 113. The node 114 (D-Glucose 6-phosphate) is also a substrate for the enzyme reaction from the node 115 to the node 116 and a product of the enzyme reaction from the node 116 to the node 115.

  Information about the enzymatic reaction from node 115 to node 116 is described in range 230 of FIG. That is, the node 115 indicates the enzyme (glucose-6-phosphate dehydrogenase) with ID “1.1.1.49”, and “NADP +” and “D-Glucose 6-phosphate”, which are substrates for this enzyme reaction, , ID “1.1.1.49” enzyme (glucose-6-phosphate dehydrogenase) and the products of this enzyme reaction “NADPH”, “h”, “D-Glucono-1”, and “5-lactone 6” -phosphate ". The Michaelis constant of this enzymatic reaction is “1.2000000000000002E-5 mmol / l”, the turnover number is “30100.0 / s”, and the specific activity is “790.0 umol / min / mg”. . This enzyme (1.1.1.49) can be collected from, for example, green pea, corn, wild boar, candida, bacteria, rats, dogs, cows, and humans. Further, the allocated amount (concentration) of this enzyme (1.1.1.49) is “5.723009684711666 nmol”. The traffic of this enzymatic reaction was “40000.0 nmol”.

  Information about the enzyme reaction from node 116 to node 115 is described in range 231 of FIG. The Michaelis constant of this enzymatic reaction is “0.014 mmol / l” and the turnover number is “10.0 / s”. The traffic of this enzyme reaction was “0.0 nmol”.

  Node 117 indicates “D-Glucono-1” and “5-lactone 6-phosphate”, which are products of the enzyme reaction from node 115 to node 116. The node 117 (D-Glucono-1 and 5-lactone 6-phosphate) is also a substrate for the enzyme reaction from the node 116 to the node 115 and a substrate for the enzyme reaction from the node 118 to the node 119.

Information about the enzyme reaction from node 118 to node 119 is described in range 226 of FIG. That is, the node 118 has an enzyme with ID “3.1.1.31” (6-phosphogluconolactonase) and “H ₂ 0”, “D-Glucono-1”, and “5-lactone 6-” that are substrates for this enzymatic reaction. The node 119 indicates an enzyme with ID “3.1.1.31” (6-phosphogluconolactonase) and “6-Phospho-D-gluconate” which is a product of this enzyme reaction. The Michaelis constant of this enzymatic reaction is “0.08 mmol / l”, the turnover number is “100.0 / s”, and the specific activity is “6753.0 umol / min / mg”. This enzyme (3.1.1.31) can be collected from, for example, rats, humans, cows, and E. coli. Moreover, the allocated amount (concentration) of this enzyme (3.1.1.31) is “7.107184800310227 nmol”. The traffic of this enzymatic reaction was “40000.0 nmol”.

  The node 120 indicates “6-Phospho-D-gluconate”, which is a product of the enzyme reaction from the node 118 to the node 119. The node 120 (6-Phospho-D-gluconate) is also a substrate for the enzyme reaction from the node 121 to the node 122.

Information about the enzyme reaction from node 121 to node 122 is described in range 236 of FIG. That is, the node 121 indicates the enzyme of ID “4.2.1.12” (phosphogluconate dehydratase) and “6-Phospho-D-gluconate” which is a substrate of the enzyme reaction, and the node 122 indicates the ID “4.2.1.12”. As well as “H ₂ 0” and “2-Dehydro-3-deoxy-6-phospho-D-gluconate”, which are the products of this enzymatic reaction. The Michaelis constant of this enzymatic reaction is “0.04 mmol / l”, and the turnover number is “100.0 / s”. This enzyme (4.2.1.12) can be collected from, for example, rhizobia, Escherichia coli, and Candida fungi. Further, the allocated amount (concentration) of the enzyme (4.2.1.12) is “3.3411991914852237 nmol”. The traffic of this enzymatic reaction was “40000.0 nmol”.

  The node 123 indicates “2-Dehydro-3-deoxy-6-phospho-D-gluconate”, which is a product of the enzyme reaction from the node 121 to the node 122. This node 123 (2-Dehydro-3-deoxy-6-phospho-D-gluconate) is also a substrate for the enzyme reaction from the node 124 to the node 125 and a substrate for the enzyme reaction from the node 125 to the node 124. is there.

  Information about the enzymatic reaction from node 124 to node 125 is described in range 234 of FIG. That is, the node 124 includes an enzyme with ID “4.1.2.14” (2-dehydro-3-deoxy-phosphogluconate aldolase) and “2-Dehydro-3-deoxy-6-phospho-D” which is a substrate of the enzyme reaction. node 125 indicates the enzyme with ID “4.1.2.14” (2-dehydro-3-deoxy-phosphogluconate aldolase) and “Pyruvate” and “(2R) −” which are the products of this enzymatic reaction. 2-Hydroxy-3- (phosphonooxy) -propanal ". The Michaelis constant of this enzyme reaction is “0.0060 mmol / l”, the turnover number is “533.0 / s”, and the specific activity is “625.0 umol / min / mg”. This enzyme (4.1.2.14) can be collected from, for example, rhizobia or Escherichia coli. Further, the allocated amount (concentration) of this enzyme (4.1.2.14) is “1.459436730959706 nmol”. The traffic of this enzyme reaction was “40000.0 nmol”.

  Information about the enzyme reaction from node 125 to node 124 is described in range 235 of FIG. The Michaelis constant of this enzymatic reaction is “10.0 mmol / l” and the turnover number is “6.0 / s”. The traffic of this enzyme reaction was “0.0 nmol”.

  Node 126 indicates “(2R) -2-Hydroxy-3- (phosphonooxy) -propanal”, which is a product of the enzyme reaction from node 124 to node 125. The node 126 ((2R) -2-Hydroxy-3- (phosphonooxy) -propana) is a substrate for the enzyme reaction from the node 125 to the node 124, a substrate for the enzyme reaction from the node 128 to the node 129, and It is also the product of the enzymatic reaction from node 129 to node 128.

Information about the enzyme reaction from node 128 to node 129 is described in range 216 of FIG. That is, the node 128 includes an enzyme (glyceraldehyde-3-phosphate dehydrogenase) having an ID “1.2.1.9” and “(2R) -2-Hydroxy-3- (phosphonooxy) -propanal”, which is a substrate of the enzyme reaction, “NADP +” and “H ₂ O” are shown, and node 129 is an enzyme (glyceraldehyde-3-phosphate dehydrogenase) having ID “1.2.1.9” and “3-Phospho-D” which is a product of this enzyme reaction. -glycerate "," NADPH ", and two" h ". The Michaelis constant of this enzyme reaction is “0.017 mmol / l”, the turnover number is “103.0 / s”, and the specific activity is “150.5 umol / min / mg”. This enzyme (1.2.1.9) can be collected from, for example, green peas, bacteria, corn, wheat, and spinach. The amount (concentration) of this enzyme (1.2.1.9) is “6.260318661362094 nmol”. The traffic of the enzyme reaction was “47510.533612162806 nmol”.

  Information about the enzyme reaction from node 129 to node 128 is described in range 217 of FIG. The Michaelis constant of this enzymatic reaction is “0.062 mmol / l” and the turnover number is “10.0 / s”. The traffic of this enzyme reaction was “7510.533612162805 nmol”.

  The node 130 indicates “3-Phospho-D-glycerate”, which is a product of the enzyme reaction from the node 128 to the node 129. This node 130 (3-Phospho-D-glycerate) is a substrate for enzyme reaction from node 129 to node 128, a product of enzyme reaction from node 137 to node 138, and an enzyme reaction from node 138 to node 137. , The substrate of the enzyme reaction from node 139 to node 140, and the product of the enzyme reaction from node 140 to node 139.

  Node 127 indicates “Pyruvate” which is a product of the enzyme reaction from node 124 to node 125. This node 126 (Pyruvate) is a substrate of the enzyme reaction from the node 125 to the node 124, a substrate of the enzyme reaction from the node 131 to the node 132, a product of the enzyme reaction from the node 132 to the node 131, and the node 162 The product of the enzyme reaction from node 163, the substrate of the enzyme reaction from node 163 to node 162, and the substrate of the enzyme reaction from node 164 to node 165.

  Information about the enzyme reaction from node 131 to node 132 is described in range 228 of FIG. That is, the node 131 indicates the enzyme (pyruvate kinase) with ID “2.7.1.40” and the substrates “ATP” and “Pyruvate” of this enzyme reaction, and the node 132 indicates the enzyme with ID “2.7.1.40”. (Pyruvate kinase) and "ADP" and "Phosphoenolpyruvate" which are products of this enzymatic reaction. The Michaelis constant of this enzymatic reaction is “0.48 mmol / l”, the turnover number is “100.0 / s”, and the specific activity is “1685.0 umol / min / mg”. This enzyme (2.7.1.40) can be collected from, for example, wild boar, bacteria, Salmonella, spinach, cows, rabbits, dogs, Euglena, humans, rats, and E. coli. Further, the allocated amount (concentration) of this enzyme (2.7.1.40) is “5.644579048497802 nmol”. The traffic of this enzyme reaction was “93983.78606942232 nmol”.

  Information about the enzyme reaction from node 132 to node 131 is described in range 229 of FIG. The Michaelis constant of this enzymatic reaction is “0.03 mmol / l”, and the turnover number is “232.0 / s”. The traffic of this enzyme reaction was “60916.44483227227 nmol”.

  The node 133 indicates “Phosphoenolpyruvate”, which is a product of the enzyme reaction from the node 131 to the node 132. This node 133 (Phosphoenolpyruvate) is also a substrate of the enzyme reaction from the node 132 to the node 131, a substrate of the enzyme reaction from the node 134 to the node 135, and a product of the enzyme reaction from the node 135 to the node 134. .

Information about the enzyme reaction from node 134 to node 135 is described in range 213 of FIG. That is, the node 134 indicates an enzyme (phosphopyruvate hydratase) having an ID “4.2.1.11”, and substrates “Phosphoenolpyruvate” and “H ₂ O” of the enzyme reaction, and the node 135 has an ID “4.2.1.11”. The enzyme (phosphopyruvate hydratase) and “2-Phospho-D-glycerate” which is a product of this enzyme reaction are shown. The Michaelis constant of this enzymatic reaction is “0.11 mmol / l”, and the turnover number is “10.0 / s”. This enzyme (4.2.1.11) can be collected from, for example, corn, wild boar, candida, rabbit, bacteria, rat, dog, cow, E. coli, and human. Further, the allocated amount (concentration) of this enzyme (4.2.1.11) is “5.677655768238286 nmol”. The traffic of this enzyme reaction was “39875.078162698206 nmol”.

  Information about the enzyme reaction from node 135 to node 134 is described in range 212 of FIG. The Michaelis constant of this enzymatic reaction is “0.0 mmol / l”, the turnover number is “230.0 / s”, and the intrinsic activity is “1118.0 umol / min / mg”. The traffic of the enzyme reaction was “6807.736925548192 nmol”.

  Node 136 indicates “2-Phospho-D-glycerate”, which is a product of the enzyme reaction from node 134 to node 135. The node 133 (2-Phospho-D-glycerate) is a substrate for the enzyme reaction from the node 135 to the node 134, a substrate for the enzyme reaction from the node 137 to the node 138, and an enzyme from the node 138 to the node 137. It is also the product of the reaction.

  Information about the enzyme reaction from node 137 to node 138 is described in range 232 of FIG. That is, the node 137 indicates an enzyme (phosphoglycerate mutase) with an ID “5.4.2.1” and “2-Phospho-D-glycerate” which is a substrate for the enzyme reaction, and the node 138 has an ID “5.4.2.1”. As well as “3-Phospho-D-glycerate” which is a product of this enzyme reaction. The product “3-Phospho-D-glycerate” is shown in the node 130 described above. Further, the Michaelis constant of this enzyme reaction is “0.041 mmol / l”, the turnover number is “199.0 / s”, and the specific activity is “2880.0 umol / min / mg”. This enzyme (5.4.2.1) can be collected from, for example, corn, wheat, wild boar, nematode, silkworm, bacteria, rat, cow, Escherichia coli, rice, human, and Candida fungus. Further, the allocated amount (concentration) of the enzyme (5.4.2.1) is “5.5627079024453545 nmol”. The traffic of the enzyme reaction was “63015.941943861675 nmol”.

  Information about the enzyme reaction from node 138 to node 137 is described in range 233 of FIG. Note that “3-Phospho-D-glycerate”, which is a substrate for this enzyme reaction, is shown in the node 130 described above. The Michaelis constant of this enzymatic reaction is “0.026 mmol / l” and the turnover number is “530.0 / s”. The traffic of this enzyme reaction was “29948.60070671166 nmol”.

Information about the enzyme reaction from node 139 to node 140 is described in range 225 of FIG. Note that the substrate of this enzyme reaction is indicated by the node 130 described above. That is, the node 139 indicates the enzyme with ID “3.1.3.38” (3-phosphoglycerate phosphatase), and “3-Phospho-D-glycerate” and “H ₂ O” which are substrates for this enzymatic reaction. Indicates the enzyme with ID “3.1.3.38” (3-phosphoglycerate phosphatase) and “D-Glycerate” and “Orthophosphate” which are products of this enzyme reaction. Further, the Michaelis constant of this enzyme reaction is “0.28 mmol / l”, the turnover number is “100.0 / s”, and the specific activity is “740.0 umol / min / mg”. This enzyme (3.1.3.38) can be collected from, for example, green pea, corn, alfalfa, and spinach. Moreover, the allocated amount (concentration) of this enzyme (3.1.3.38) is “2.938928995971154 nmol”. The traffic of the enzyme reaction was “73067.34123715002 nmol”.

  The node 141 indicates “Orthophosphate” which is a product of the enzyme reaction from the node 139 to the node 140. A node 142 indicates “D-Glycerate”, which is a product of the enzyme reaction from the node 139 to the node 140. The node 142 (D-Glycerate) is also a substrate for the enzyme reaction from the node 143 to the node 144 and a product of the enzyme reaction from the node 144 to the node 143.

  Information about the enzyme reaction from node 143 to node 144 is described in range 218 of FIG. That is, the node 143 indicates the enzyme (hydroxypyruvate reductase) with ID “1.1.1.81”, and “D-Glycerate” and “NADP +”, which are substrates of this enzyme reaction, and the node 144 has the ID “1.1.1.81”. The enzyme (hydroxypyruvate reductase) and “Hydroxypyruvate”, “NADPH” and “h” which are products of this enzyme reaction are shown. The Michaelis constant of this enzyme reaction is “0.037 mmol / l”, the turnover number is “100.0 / s”, and the specific activity is “943.0 umol / min / mg”. This enzyme (1.1.1.81) can be collected from, for example, green pea, corn, rat, wild boar, cow, and spinach. Further, the allocated amount (concentration) of this enzyme (1.1.1.81) is “20.00797589129738 nmol”. The traffic of this enzyme reaction was “354833.7646339715 nmol”.

  Information about the enzyme reaction from node 144 to node 143 is described in range 219 of FIG. The Michaelis constant of this enzymatic reaction is “0.015 mmol / l”, and the turnover number is “10.0 / s”. The traffic of this enzyme reaction was “281766.4233968215 nmol”.

  Node 145 indicates “Hydroxypyruvate” which is a product of the enzyme reaction from node 143 to node 144. The node 145 (Hydroxypyruvate) is also a substrate for the enzyme reaction from the node 144 to the node 143 and a substrate for the enzyme reaction from the node 146 to the node 147.

Information about the enzyme reaction from node 146 to node 147 is described in range 227 of FIG. That is, the node 146 indicates the enzyme (hydroxypyruvate decarboxylase) with ID “4.1.1.40” and “Hydroxypyruvate”, which is a substrate for this enzyme reaction, and the node 147 indicates the enzyme (hydroxypyruvate decarboxylase) with ID “4.1.1.40”. And “Glycolaldehyde” and “CO ₂ ” which are products of this enzymatic reaction. The Michaelis constant of this enzymatic reaction is “1.0 mmol / l”, and the turnover number is “100.0 / s”. This enzyme (4.1.1.40) can be collected from, for example, dogs, cows, rabbits, rats, and boars. Further, the allocated amount (concentration) of the enzyme (4.1.1.40) is “4.032799046786325 nmol”. The traffic of the enzyme reaction was “73067.34123715002 nmol”.

  Node 148 indicates “Glycolaldehyde” which is the product of the enzymatic reaction from node 146 to node 147. The node 148 (Glycolaldehyde) is also a substrate for the enzyme reaction from the node 149 to the node 151 and a substrate for the enzyme reaction from the node 151 to the node 149.

  Further, the node 150 indicates “NAD +” which is a substrate of the enzyme reaction from the node 149 to the node 151 and a product of the enzyme reaction from the node 151 to the node 149.

Information about the enzyme reaction from node 149 to node 151 is described in range 214 of FIG. That is, the node 149 indicates an enzyme (glycolaldehyde dehydrogenase) with ID “1.2.1.21” and “Glycolaldehyde”, “NAD +”, and “H ₂ O” that are substrates of this enzyme reaction, and node 151 has ID ID “1.2.1.21” enzyme (glycolaldehyde dehydrogenase), and “Glycolate”, “NADH”, and two “h”, which are products of this enzyme reaction, are shown. The Michaelis constant of this enzymatic reaction is “0.027 mmol / l”, the turnover number is “100.0 / s”, and the specific activity is “30.5 umol / min / mg”. This enzyme (1.2.1.21) can be collected from bacteria, Salmonella, Escherichia coli, and the like. Further, the allocated amount (concentration) of this enzyme (1.2.1.21) is “7.061585889861108 nmol”. The traffic of the enzyme reaction was “105296.45600275489 nmol”.

  Information about the enzyme reaction from node 151 to node 149 is described in range 215 of FIG. The Michaelis constant of this enzymatic reaction is “5.9000000000000025E-8 mmol / l”, and the turnover number is “10.0 / s”. The traffic of the enzyme reaction was “32229.114765604863 nmol”.

  The node 152 indicates a product of the enzyme reaction from the node 149 to the node 151 and “NADH” which is a substrate of the enzyme reaction from the node 151 to the node 149.

  A node 153 indicates a product of the enzyme reaction from the node 149 to the node 151 and “Glycolate” which is a substrate of the enzyme reaction from the node 151 to the node 149. This node 153 (Glycolate) is also a substrate for the enzyme reaction from the node 154 to the node 156.

  Information about the enzyme reaction from node 154 to node 156 is described in range 220 of FIG. That is, the node 154 indicates the enzyme (glycolate dehydrogenase) with ID “1.1.99.14”, and “Glycolate” and “Acceptor”, which are substrates of this enzyme reaction, and the node 156 indicates the enzyme with ID “1.1.99.14”. (Glycolate dehydrogenase) and “Glyoxylate” and “Reduced acceptor” which are products of this enzymatic reaction. The Michaelis constant of this enzymatic reaction is “0.04 mmol / l”, the turnover number is “100.0 / s”, and the specific activity is “3.1 umol / min / mg”. This enzyme (1.1.99.14) can be collected from, for example, Donariella algae, Euglena, and Arabidopsis. Moreover, the allocated amount (concentration) of this enzyme (1.1.99.14) is “6.219569206751489 nmol”. The traffic of the enzyme reaction was “73067.34123715002 nmol”.

  A node 155 indicates “Acceptor” which is a substrate of the enzyme reaction from the node 154 to the node 156.

  The node 157 indicates “Reduced acceptor” that is a product of the enzyme reaction from the node 154 to the node 156.

  Node 158 shows “Glyoxylate” which is the product of the enzymatic reaction from node 154 to node 156. This node 158 (Glyoxylate) is also a substrate for the enzyme reaction from the node 159 to the node 160.

Information about the enzyme reaction from node 159 to node 160 is described in range 221 of FIG. That is, node 159 shows the enzyme (malate synthase) with ID “2.3.3.9” and the substrates of this enzyme reaction “Acetyl-CoA”, “H ₂ O”, and “Glyoxylate”. , ID (2.3.3.9) enzyme (malate synthase), and products of this enzyme reaction, “(S) -Malate” and “CoA”. The Michaelis constant of this enzymatic reaction is “5.9E-4 mmol / l”, the turnover number is “161.0 / s”, and the specific activity is “25090.0 umol / min / mg”. This enzyme (2.3.3.9) can be collected from, for example, Donariella algae, Euglena, and Arabidopsis thaliana. Further, the allocated amount (concentration) of the enzyme (2.3.3.9) is “6.1659687812423245 nmol”. The traffic of the enzyme reaction was “73067.34123715002 nmol”.

  The node 161 indicates “(S) -Malate” which is a product of the enzyme reaction from the node 159 to the node 160. The node 161 ((S) -Malate) is also a substrate for the enzyme reaction from the node 162 to the node 163 and a product of the enzyme reaction from the node 163 to the node 162.

Information about the enzyme reaction from node 162 to node 163 is described in range 222 of FIG. That is, the node 162 indicates the enzyme (malate dehydrogenase) with the ID “1.1.1.40”, and “(S) -Malate” and “NADP +” which are substrates of the enzyme reaction, and the node 163 has the ID “1.1. 1.40 "enzyme (malate dehydrogenase) and" Pyruvate "," CO ₂ ", and" NADPH "which are the products of this enzymatic reaction. The product “Pyruvate” is shown in the node 127 described above. The Michaelis constant of this enzymatic reaction is “0.00118 mmol / l”, the turnover number is “582.0 / s”, and the intrinsic activity is “7910.0 umol / min / mg”. This enzyme (1.1.1.40) can be collected from, for example, corn, wild boar, rabbit, rhizobia, human, wheat, rat, and cow. Further, the allocated amount (concentration) of this enzyme (1.1.1.40) is “5.307051508393477 nmol”. The traffic of the enzyme reaction was “73067.34123715002 nmol”.

  Information about the enzyme reaction from node 163 to node 162 is described in range 223 of FIG. The Michaelis constant of this enzymatic reaction is “0.0020 mmol / l”, and the turnover number is “10.0 / s”. The traffic of this enzyme reaction was “0.0 nmol”.

Information about the enzyme reaction from node 164 to node 165 is described in range 224 of FIG. That is, the node 164 indicates the enzyme (pyruvate dehydrogenase) with ID “1.2.1.51” and the substrates of the enzyme reaction “Pyruvate”, “CoA”, and “NADP +”, and the node 165 has the ID “1.2”. .1.51 "(pyruvate dehydrogenase) and the products of this enzymatic reaction," Acetyl-CoA "," CO ₂ ", and" NADPH ". This substrate “Pyruvate” is shown in the node 127 described above. The Michaelis constant of this enzymatic reaction is “0.0066 mmol / l”, the turnover number is “100.0 / s”, and the intrinsic activity is “15.3 umol / min / mg”. This enzyme (1.2.1.51) can be collected from, for example, Euglena. Further, the allocated amount (concentration) of the enzyme (1.2.1.51) is “1.145061623996569 nmol”. The traffic of the enzyme reaction was “80000.0 nmol”.

  Node 166 indicates “Acetyl-CoA” which is a product of the enzyme reaction from node 164 to node 165. This node 166 (Acetyl-CoA) is also a substrate for the enzyme reaction from the node 159 to the node 160.

A simulation result of the configuration as described above is shown in a range 237 of FIG. When the starting material was “D-Glucose” and the emission material was “CO ₂ ” and the emission amount after 60 minutes was calculated, the maximum value of the emission amount was “226134.6824743001 nmol”.

  The efficiency of this enzyme network 100 is compared to the pentose phosphate cycle, which is a known metabolic pathway.

  FIG. 11 is a diagram illustrating a configuration example of a pentose phosphate circuit. In FIG. 11, the description method of the pentose phosphate circuit 300 is basically the same as that of the enzyme network 100 of FIG.

  The simulation results of the pentose phosphate circuit 300 of FIG. 11 are shown in FIGS. The configuration of the pentose phosphate circuit 300 will be described more specifically with reference to these.

  The list described in the range 401 in FIG. 12 is a list of enzyme reactions performed in the pentose phosphate circuit 300. Since the described format is the same as in the case of FIG.

  A range 402 in FIG. 12 shows the final product (exhaust substance) and its concentration (exhaust amount).

  Details of the enzyme reaction are shown in FIGS. The configurations of the ranges 411 to 427 in FIGS. 13 to 17 are basically the same as those in FIGS. 3 to 10.

  The configuration of FIG. 11 will be described with reference to ranges 411 to 427 in which information is described in the above configuration.

  In FIG. 11, a node 311 is “D-Glucose” which is a starting material and is a substrate of an enzyme reaction from the node 313 to the node 314. The concentration of the starting material is “40000.0 nmol” as in the case of the enzyme network 100.

  A node 312 indicates “ATP” which is a substrate of an enzyme reaction from the node 313 to the node 314.

  Information about the enzyme reaction from the node 313 to the node 314 is described in a range 413 in FIG. The node 313 indicates an enzyme (glucokinase) with an ID “2.7.1.2” and substrates “D-Glucose” and “ATP” of the enzyme reaction, and a node 314 indicates an ID “2.7.1.2” (glucokinase). And "ADP" and "D-Glucose 6-phosphate" which are products of this enzyme reaction. The traffic of this enzymatic reaction was “40000.0 nmol”.

  Node 315 indicates “ADP” which is a product of the enzyme reaction from node 313 to node 314.

  The node 316 indicates “D-Glucose 6-phosphate” which is a product of the enzyme reaction from the node 313 to the node 314. Note that this node (D-Glucose 6-phosphate) is a substrate for the enzyme reaction from node 317 to node 318, a product of the enzyme reaction from node 318 to node 317, and an enzyme reaction from node 345 to node 346. As well as the substrate of the enzymatic reaction from node 346 to node 345.

  Information about the enzyme reaction from node 317 to node 318 is described in range 421 in FIG. Node 317 indicates an enzyme (glucose-6-phosphate dehydrogenase) with ID “1.1.1.49”, and substrates “NADP +” and “D-Glucose 6-phosphate” of this enzyme reaction. “1.1.1.49” enzyme (glucose-6-phosphate dehydrogenase) and the products of this enzyme reaction “NADPH”, “h”, “D-Glucono-1”, and “5-lactone 6-phosphate” Is shown. Moreover, the allocated amount (concentration) of this enzyme (1.1.1.49) is “0.974925718932978 nmol”. The traffic of this enzyme reaction was “107162.98046962103 nmol”.

  Information about the enzyme reaction from node 318 to node 317 is described in range 422 of FIG. The traffic of this enzyme reaction was “10524.11222672474 nmol”.

  Node 319 indicates “h”, which is the product of the enzymatic reaction from node 317 to node 318. This node 319 (h) is also a substrate for the enzyme reaction from the node 318 to the node 317.

  Node 320 shows “D-Glucono-1” and “5-lactone 6-phosphate” which are products of the enzyme reaction from node 317 to node 318. This node 320 (D-Glucono-1 and 5-lactone 6-phosphate) is also a substrate for the enzyme reaction from the node 322 to the node 323.

The node 321 indicates “H ₂ O” which is a substrate of the enzyme reaction from the node 322 to the node 323.

Information about the enzyme reaction from node 322 to node 323 is described in range 416 of FIG. The node 322 includes an enzyme with ID “3.1.1.31” (6-phosphogluconolactonase) and “H ₂ 0”, “D-Glucono-1”, and “5-lactone 6-phosphate” which are substrates for this enzymatic reaction. The node 323 indicates an enzyme with ID “3.1.1.31” (6-phosphogluconolactonase) and “6-Phospho-D-gluconate” which is a product of this enzyme reaction. Further, the allocated amount (concentration) of the enzyme (3.1.1.31) is “7.7214390937079305 nmol”. The traffic of this enzyme reaction was “96638.8682428963 nmol”.

  A node 324 indicates “6-Phospho-D-gluconate”, which is a product of an enzyme reaction from the node 322 to the node 323. The node 324 (6-Phospho-D-gluconate) is also a substrate for the enzyme reaction from the node 325 to the node 326 and a product of the enzyme reaction from the node 326 to the node 325.

Information about the enzyme reaction from node 325 to node 326 is described in range 414 of FIG. Node 325 shows an enzyme (phosphogluconate dehydrogenase) with ID “1.1.1.44” and substrates of this enzyme reaction, “6-Phospho-D-gluconate” and “NADP +”, and node 326 shows ID “1.1. 1.44 "of an enzyme (phosphogluconate dehydrogenase), as well as a product of the enzymatic reaction" D-Ribulose "," 5-phosphate "indicates" CO ₂ ", and" NADPH ". The Michaelis constant of this enzyme reaction is “0.0060 mmol / l”, the turnover number is “98.0 / s”, and the specific activity is “175.0 umol / min / mg”. This enzyme (1.1.1.44) can be collected from, for example, green pea, rat, wild boar, bacteria, silkworm, Salmonella, human, spinach, Candida, rice, and Escherichia coli. Further, the allocated amount (concentration) of this enzyme (1.1.1.44) is “1.032908096565134 nmol”. The traffic of this enzyme reaction was “96638.8682428963 nmol”.

  Information about the enzyme reaction from node 326 to node 325 is described in range 415 of FIG. The Michaelis constant of this enzymatic reaction is “2.2E-4 mmol / l”, and the turnover number is “10.0 / s”. The traffic of this enzyme reaction was “0.0 nmol”.

Node 327 indicates “CO ₂ ” which is the product of the enzyme reaction from node 325 to node 326. This node 327 (CO ₂ ) is also a substrate for the enzyme reaction from the node 326 to the node 325.

  Node 328 indicates “D-Ribulose 5-phosphate” which is a product of the enzyme reaction from node 325 to node 326. In addition, this node 328 (D-Ribulose 5-phosphate) is a substrate of the enzyme reaction from the node 329 to the node 330, a substrate from the node 332 to the node 333, and a product of the enzyme reaction from the node 333 to the node 332 But there is.

  Information about the enzyme reaction from node 329 to node 330 is described in range 427 of FIG. The node 329 indicates an enzyme (ribulose-phosphate 3-epimerase) with an ID “5.1.3.1” and “D-Ribulose 5-phosphate” which is a substrate for this enzyme reaction, and the node 330 has an ID “5.1.3.1”. And the enzyme "ribulose-phosphate 3-epimerase" and "D-Xylulose 5-phosphate" which is a product of this enzyme reaction. The Michaelis constant of this enzyme reaction is “0.19 mmol / l”, the turnover number is “7100.0 / s”, and the specific activity is “11610.0 umol / min / mg”. This enzyme (5.1.3.1) can be collected from, for example, rice, bacteria, rats, spinach, cattle, Escherichia coli, rabbits, rice, and humans. Moreover, the allocated amount (concentration) of this enzyme (5.1.3.1) is “62.774954936062876 nmol”. The traffic of this enzyme reaction was “68319.43412144815 nmol”.

  The node 331 indicates “D-Xylulose 5-phosphate” that is a product of the enzyme reaction from the node 329 to the node 330. This node 331 (D-Xylulose 5-phosphate) is a substrate for the enzyme reaction from the node 335 to the node 336, a product of the enzyme reaction from the node 336 to the node 335, and an enzyme reaction from the node 339 to the node 341. It is also the substrate and the product of the enzymatic reaction from node 341 to node 339.

  Information about the enzyme reaction from the node 332 to the node 333 is described in a range 411 in FIG. The node 332 indicates an enzyme (ribose-5-phosphate isomerase) having an ID “5.3.1.6” and “D-Ribulose 5-phosphate” which is a substrate of the enzyme reaction, and the node 333 has an ID “5.3.1.6”. "Enzyme" (ribose-5-phosphate isomerase) and "D-Ribulose 5-phosphate" which is a product of this enzyme reaction. The Michaelis constant of this enzymatic reaction is “0.108 mmol / l”, the turnover number is “3440.0 / s”, and the specific activity is “1700.0 umol / min / mg”. This enzyme (5.3.1.6) can be collected from, for example, green pea, rat, wild boar, cow, Escherichia coli, human, Candida, spinach and the like. Further, the allocated amount (concentration) of the enzyme (5.3.1.6) is “13.091980787699258 nmol”. The traffic of this enzyme reaction was “22503.965709252243 nmol”.

  Information about the enzyme reaction from node 333 to node 332 is described in range 412 of FIG. The Michaelis constant of this enzymatic reaction is “0.66 mmol / l” and the turnover number is “50.0 / s”. The traffic of the enzyme reaction was “50823.399830700386 nmol”.

  Node 334 indicates “D-Ribulose 5-phosphate”, which is a product of the enzyme reaction from node 332 to node 333. This node 334 (D-Ribulose 5-phosphate) is a substrate for enzyme reaction from node 333 to node 332, a substrate for enzyme reaction from node 335 to node 336, and an enzyme reaction from node 336 to node 335. It is also the product of

  Information about the enzyme reaction from node 335 to node 336 is described in range 425 of FIG. The node 335 indicates an enzyme (transketolase) having an ID “2.2.1.1”, and “D-Ribose 5-phosphate” and “D-Xylulose 5-phosphate” which are substrates of the enzyme reaction. “2.2.1.1” enzyme (transketolase) and “Sedoheptulose 7-phosphate” and “(2R) -2-Hydroxy-3- (phosphonooxy) -propanal” which are products of this enzyme reaction are shown. The Michaelis constant of this enzyme reaction is “4.0 mmol / l”, the turnover number is “100.0 / s”, and the specific activity is “50.4 umol / min / mg”. This enzyme (2.2.1.1) can be collected from, for example, rat, wheat, wild boar, E. coli, rabbit, human, Candida, spinach and the like. Further, the allocated amount (concentration) of this enzyme (2.2.1.1) is “6.4130119777843735 nmol”. The traffic of this enzyme reaction was “16896.943255219718 nmol”.

  Information about the enzyme reaction from node 336 to node 335 is described in range 426 of FIG. The Michaelis constant of this enzymatic reaction is “0.0056 mmol / l” and the turnover number is “56.7 / s”. The traffic of this enzyme reaction was “45216.37737666786 nmol”.

  Node 337 indicates “(2R) -2-Hydroxy-3- (phosphonooxy) -propanal”, which is a product of the enzyme reaction from node 335 to node 336. The node 337 ((2R) -2-Hydroxy-3- (phosphonooxy) -propanal) is a substrate of the enzyme reaction from the node 336 to the node 335 and a product of the enzyme reaction from the node 339 to the node 341. , The product of the enzyme reaction from node 339 to node 341, the substrate of the enzyme reaction from node 341 to node 339, the substrate of the enzyme reaction from node 343 to node 344, and the enzyme reaction from node 344 to node 343 It is also a product.

  Node 338 indicates “Sedoheptulose 7-phosphate”, which is a product of the enzyme reaction from node 335 to node 336. The node 338 (Sedoheptulose 7-phosphate) is also a substrate for the enzyme reaction from the node 343 to the node 344 and a product of the enzyme reaction from the node 344 to the node 343.

  Information about the enzyme reaction from the node 339 to the node 341 is described in a range 423 in FIG. The node 339 indicates the enzyme (transketolase) with ID “2.2.1.1” and “D-Erythrose 4-phosphate” and “D-Xylulose 5-phosphate” which are substrates for this enzymatic reaction. “2.2.1.1” enzyme (transketolase) and “(2R) -2-Hydroxy-3- (phosphonooxy) -propanal” and “D-Fructose 6-phosphate” which are products of this enzyme reaction are shown. The Michaelis constant of this enzyme reaction is “0.0056 mmol / l”, the turnover number is “69.0 / s”, and the specific activity is “50.4 umol / min / mg”. Further, the allocated amount (concentration) of this enzyme (2.2.1.1) is “6.4130119777843735 nmol”. The traffic of this enzyme reaction was “93511.79261905616 nmol”.

  Information about the enzyme reaction from node 341 to node 339 is described in range 424 in FIG. The Michaelis constant of this enzymatic reaction is “4.9 mmol / l” and the turnover number is “10.0 / s”. The traffic of this enzyme reaction was “65192.35849760802 nmol”.

  Node 340 indicates “D-Erythrose 4-phosphate”, which is a substrate for the enzyme reaction from node 339 to node 341. The node 340 (D-Erythrose 4-phosphate) is a product of an enzyme reaction from the node 341 to the node 339, a product of an enzyme reaction from the node 343 to the node 344, and a node 343 to the node 343. It is also a substrate for enzyme reactions.

  The node 342 indicates “D-Fructose 6-phosphate” which is a product of the enzyme reaction from the node 339 to the node 341. This node 342 (D-Fructose 6-phosphate) is a substrate of the enzyme reaction from the node 341 to the node 339, a product of the enzyme reaction from the node 343 to the node 344, and an enzyme reaction from the node 344 to the node 343. It is also the substrate, the substrate of the enzyme reaction from node 345 to node 346, and the product of the enzyme reaction from node 346 to node 345.

  Information about the enzyme reaction from node 343 to node 344 is described in range 417 of FIG. The node 343 receives the ID (2.2.1.2) enzyme (transaldolase) and “Sedoheptulose 7-phosphate” and “(2R) -2-Hydroxy-3- (phosphonooxy) -propanal” which are substrates for this enzyme reaction. Node 344 shows an enzyme (transaldolase) with ID “2.2.1.2” and “D-Erythrose 4-phosphate” and “D-Fructose 6-phosphate” which are products of this enzyme reaction. The Michaelis constant of this enzymatic reaction is “0.038 mmol / l”, the turnover number is “100.0 / s”, and the specific activity is “60.0 umol / min / mg”. This enzyme (2.2.1.2) can be collected from, for example, Euglena, Rats, cattle, E. coli, rabbits, humans, Candida and spinach. Further, the allocated amount (concentration) of this enzyme (2.2.1.2) is “0.9861131028717981 nmol”. The traffic of this enzyme reaction was “38921.48722484376 nmol”.

  Information about the enzyme reaction from node 344 to node 343 is described in range 418 of FIG. The Michaelis constant of this enzymatic reaction is “0.2 mmol / l”, and the turnover number is “10.0 / s”. The traffic of this enzyme reaction was “10602.053103395614 nmol”.

Information about the enzyme reaction from node 345 to node 346 is described in range 419 of FIG. The node 345 indicates an enzyme (glucose-6-phosphate isomerase) with an ID “5.3.1.9” and “D-Glucose 6-phosphate” which is a substrate for the enzyme reaction, and the node 346 has an ID “5.3.1.9”. "Enzyme" (glucose-6-phosphate isomerase) and "D-Fructose 6-phosphate" which is a product of this enzyme reaction. Further, the Michaelis constant of this enzyme reaction is “0.03 mmol / l”, the turnover number is “42.0 / s”, and the specific activity is “1470.0 umol / min / mg”. This enzyme (5.3.1.9) can be collected from, for example, green pea, wild boar, rabbit, dog, human, spinach, wheat, bacteria, rat, cow, and E. coli. Further, the allocated amount (concentration) of this enzyme (5.3.1.9) is “4.943054351198328 nmol”. The traffic of this enzyme reaction was “49675.42881604301 nmol”.

  Information about the enzyme reaction from node 346 to node 345 is described in range 420 of FIG. In addition, the Michaelis constant of this enzyme reaction is “0.01 mmol / l”, and the turnover number is “3330.0 / s”. The traffic of this enzyme reaction was “106314.2970589393 nmol”.

A result of simulating the pentose phosphate circuit 300 configured as described above is shown in a range 428 of FIG. When the starting material was “D-Glucose” and the emission material was “CO ₂ ” and the emission amount after 60 minutes was calculated, the maximum value of the emission amount was “96638.8682428963 nmol”.

As shown in the range 237 of FIG. 10, in the case of the enzyme network 100, the maximum value of the discharge amount is “226134.6824743001 nmol”, so the enzyme network 100 is more than twice as efficient as the pentose phosphate circuit 300. It produces and emits CO ₂ . That is, the enzyme network 100 can generate electric energy more efficiently than the pentose phosphate circuit 300 which is a known metabolic circuit.

Theoretically, six CO ₂ molecules can be generated from one glucose molecule. That is, 240000 nmol of CO ₂ can be generated theoretically from 40000 nmol of glucose. As shown in the simulation results described above, the enzyme network 100 can metabolize almost all glucose to CO ₂ in as little as 60 minutes. In the natural enzyme network such as the pentose phosphate circuit 300, characteristics (storage, redundancy, etc.) suitable for life activities are required. Therefore, there is still a network that demands pure metabolic efficiency like the enzyme network 100. Not found. That is, the enzyme network 100 can generate electrical energy more efficiently than known enzyme networks existing in nature.

  Unlike the case of the pentose phosphate circuit 300, the enzyme network 100 includes an enzyme with ID “4.2.1.12” (phosphogluconate dehydratase) and an enzyme with ID “4.1.2.14” (2-dehydro-3-deoxy-phosphogluconate aldolase). Used to metabolize 6-Phospho-D-gluconate to Pyruvate and (2R) -2-Hydroxy-3- (phosphonooxy) -propanal.

By generating CO ₂ from this pyruvate and (2R) -2-Hydroxy-3- (phosphonooxy) -propanal, it is possible to form an enzyme network that generates CO ₂ at multiple locations as described above. it can. As a result, the number of chemical reactions that emit electrons also increases, so that the enzyme network 100 can efficiently generate electrical energy.

In other words, the enzyme network 100 is a first enzyme network consisting of a plurality of enzymes that catalyze a series of chemical reactions that metabolize D-Glucose to 6-Phospho-D-gluconate, similar to the pentose phosphate circuit 300, ID "4.2.1.12" enzyme (phosphogluconate dehydratase), ID "4.1.2.14" enzyme (2-dehydro-3-deoxy-phosphogluconate aldolase), and Pyruvate and (2R) -2-Hydroxy-3- (phosphonooxy) It is only necessary to have a second enzyme network consisting of a plurality of enzymes that catalyze a series of chemical reactions that metabolize -propanal to CO _2. The first enzyme network and the second enzyme network are illustrated in FIG. It may be composed of an enzyme other than the enzyme group to be produced.

However, in this second enzyme network, as shown in the example of FIG. 1, (2R) -2 produced by being catalyzed by the enzyme with ID “4.1.2.14” (2-dehydro-3-deoxy-phosphogluconate aldolase) -Hydroxy-3- (phosphonooxy) -propanal, NADP + and H2O metabolize to 3-Phospho-D-glycerate, NADPH, h, and h. Enzyme with ID “1.2.1.9” (glyceraldehyde- By using 3-phosphate dehydrogenase), an enzyme network that generates CO ₂ can be formed at a plurality of locations. Moreover, a pathway for generating pyruvate from 3-Phospho-D-glycerate can also be constructed, and as described later, metabolic efficiency can be improved.

  The enzyme (glyceraldehyde-3-phosphate dehydrogenase) with ID “1.2.1.9” is basically an enzyme that can be collected only from plants such as green peas, wheat, or spinach. It is basically impossible in nature for such plant enzymes to construct one enzyme network with enzymes collected from animals. The enzyme network 100 can generate electric energy more efficiently by applying such a combination of enzymes that does not exist in nature.

This second enzyme network is (2R) -2-Hydroxy-3- (phosphonooxy) produced by catalysis by the enzyme with ID “4.1.2.14” (2-dehydro-3-deoxy-phosphogluconate aldolase). It includes a third enzyme network consisting of multiple enzymes that catalyze a series of chemical reactions that metabolize -propanal into multiple CO ₂ and also metabolize into pyruvate. By such a third network, (2R) -2-Hydroxy-3- (phosphonooxy)-produced by catalyzing the enzyme with ID “4.1.2.14” (2-dehydro-3-deoxy-phosphogluconate aldolase) Propanal and Pyruvate can be efficiently metabolized to CO ₂ .

  Therefore, this third enzyme network may be formed using enzymes other than the enzyme group exemplified in FIG. In the example of FIG. 1, the third enzyme network includes an enzyme with ID “1.2.1.9” (glyceraldehyde-3-phosphate dehydrogenase), an enzyme with ID “3.1.3.38” (3-phosphoglycerate phosphatase), and an ID “1.1”. .1.81 "enzyme (hydroxypyruvate reductase), ID" 4.1.1.40 "enzyme (hydroxypyruvate decarboxylase), ID" 1.2.1.21 "enzyme (glycolaldehyde dehydrogenase), ID" 1.1.99.14 "enzyme (glycolate dehydrogenase), ID It contains an enzyme (malate synthase) of “2.3.3.9” and an enzyme (malate dehydrogenase) of ID “1.1.1.40”.

In addition, by making the third network contain the enzyme with ID “1.2.1.51” (pyruvate dehydrogenase), in the chemical reaction catalyzed by the enzyme with ID “2.3.3.9” (malate synthase), Can supplement some Acetyl-CoA. Thereby, the enzyme network 100 suppresses deficiency of Acetyl-CoA, and the chemical reaction catalyzed by the enzyme (malate synthase) with ID “2.3.3.9” and the enzyme (malate dehydrogenase) with ID “1.1.1.40” The catalyzed chemical reaction can be promoted. Thus, the enzyme network 100, can improve the metabolic efficiency of the CO _2, can be produced more efficiently electric energy.

Furthermore, the third network is a metabolic pathway comprising an enzyme with ID “5.4.2.1” (phosphoglycerate mutase), an enzyme with ID “4.2.1.11” (phosphopyruvate hydratase), and an enzyme with ID “2.7.1.40” (pyruvate kinase). Pyruvate can be supplemented by including. Thereby, the enzyme network 100 can balance the reaction rate of each enzyme reaction in the third enzyme network so as to improve the metabolic efficiency of CO ₂ , and can generate electric energy more efficiently. .

  FIG. 18 is a cross-sectional view showing a main configuration example of such a biofuel cell using the enzyme network 100.

The biofuel cell 500 in FIG. 18 is an enzyme fuel cell that uses electrons generated when glucose is metabolized by carbon dioxide (CO ₂ ) as an electromotive force. As shown in FIG. 18, the inside of the housing 611 of the biofuel cell 500 is hollow, and an anode 521 and a cathode 523 are provided. Further, glucose and enzyme network 100 are disposed on the anode side 512 of the cavity. In such a state, the enzyme reaction as described above occurs on the anode side 512, electrons are released, and electrons accumulate in the anode 521. Further, when hydrogen ions (H +) and oxygen molecules (O ₂ ) are chemically reacted on the cathode side 513 to generate water (H ₂ O) and electrons are consumed on the cathode side 513, the anode 521 and A potential difference occurs with the cathode 523. Therefore, when the anode 521 and the cathode 513 are connected to each other via the resistor 522 outside the housing 511, a potential difference occurs between both ends of the resistor 522, and a current flows.

  Such a biofuel cell 500 conventionally uses an enzyme network existing in nature such as the pentose phosphate circuit 300. However, the biofuel cell 500 is more efficient in metabolism (generates electric energy efficiently). By using the enzyme network 100 as shown in FIG. 1, the power generation efficiency can be improved.

  In the above description, the biofuel cell has been described as the method of using the enzyme network 100, but the method of using the enzyme network 100 is arbitrary.

  Further, in this specification, the system represents the entire apparatus composed of a plurality of devices (apparatuses). The embodiment of the present invention is not limited to the above-described embodiment, and various modifications can be made without departing from the gist of the present invention.

It is a figure which shows the structural example of the enzyme network to which this invention is applied. It is a figure which shows a simulation result. It is a figure which shows the simulation result of the enzyme network 100 of FIG. It is a figure which shows the simulation result of the enzyme network 100 of FIG. It is a figure which shows the simulation result of the enzyme network 100 of FIG. It is a figure which shows the simulation result of the enzyme network 100 of FIG. It is a figure which shows the simulation result of the enzyme network 100 of FIG. It is a figure which shows the simulation result of the enzyme network 100 of FIG. It is a figure which shows the simulation result of the enzyme network 100 of FIG. It is a figure which shows the simulation result of the enzyme network 100 of FIG. It is a figure which shows the structural example of a pentose phosphate circuit. It is a figure which shows the simulation result of the pentose phosphate circuit. It is a figure which shows the simulation result of the pentose phosphate circuit. It is a figure which shows the simulation result of the pentose phosphate circuit. It is a figure which shows the simulation result of the pentose phosphate circuit. It is a figure which shows the simulation result of the pentose phosphate circuit. It is a figure which shows the simulation result of the pentose phosphate circuit. It is a figure which shows the structural example of the biofuel cell to which this invention is applied.

Explanation of symbols

  100 enzyme network, 300 pentose phosphate circuit, 500 biofuel cell, 511 housing, 521 anode, 522 resistance, 523 cathode

Claims (7)

An enzyme network consisting of multiple enzymes that catalyzes a series of chemical reactions that metabolize glucose (D-Glucose) to carbon dioxide (CO ₂ ),
A first enzyme network comprising a plurality of enzymes that catalyze a series of chemical reactions that metabolize D-Glucose to 6-Phospho-D-gluconate;
Phosphogluconate catalyzing a chemical reaction in which 6-Phospho-D-gluconate produced by catalysis by the first enzyme network is metabolized to 2-Dehydro-3-deoxy-6-phospho-D-gluconate and H ₂ O dehydratase (EC number 4.2.1.12),
2-Dehydro-3-deoxy-6-phospho-D-gluconate produced by catalyzing the phosphogluconate dehydratase (EC No. 4.2.1.12) is converted into Pyruvate and (2R) -2-Hydroxy-3- (phosphonooxy)- 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14) catalyzing the chemical reaction metabolized to propanal,
A series of metabolizing Pyruvate and (2R) -2-Hydroxy-3- (phosphonooxy) -propanal catalyzed by the 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14) to CO ₂ A second enzyme network comprising a plurality of enzymes that catalyze a chemical reaction. The second enzyme network is:
(2R) -2-Hydroxy-3- (phosphonooxy) -propanal, NADP +, and H ₂ O produced by catalysis of the 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14), 3 The enzyme network according to claim 1, comprising -Phospho-D-glycerate, NADPH, h, and glyceraldehyde-3-phosphate dehydrogenase (EC number 1.2.1.9) that catalyzes a chemical reaction metabolized to h. The second enzyme network is:
Metabolizing (2R) -2-Hydroxy-3- (phosphonooxy) -propanal produced by catalyzing the 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14) into a plurality of CO ₂ , The enzyme network according to claim 1, further comprising a third enzyme network comprising a plurality of enzymes that catalyze a series of chemical reactions that are also metabolized by pyruvate. The third enzyme network is:
(2R) -2-Hydroxy-3- (phosphonooxy) -propanal, NADP +, and H ₂ O produced by catalysis of the 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14), 3 -Phospho-D-glycerate, NADPH, h, and glyceraldehyde-3-phosphate dehydrogenase (EC number 1.2.1.9) that catalyzes the chemical reaction metabolized to h,
3-phosphoglycerate that catalyzes a chemical reaction that metabolizes 3-phosphos-D-glycerate and H ₂ O produced by catalyzing the glyceraldehyde-3-phosphate dehydrogenase (EC number 1.2.1.9) to D-Glycerate and orthophosphate phosphatase (EC number 3.1.3.38),
Hydroxypyruvate reductase (EC number 1.1.1.81) that catalyzes a chemical reaction that metabolizes D-Glycerate and NADP + produced by catalyzing the 3-phosphoglycerate phosphatase (EC number 3.1.3.38) to Hydroxypyruvate, NADPH, and h. ,
Hydroxypyruvate catalyzed by the hydroxypyruvate reductase (EC number 1.1.1.81), hydroxypyruvate decarboxylase (EC number 4.1.1.40) that catalyzes a chemical reaction that metabolizes Glycolaldehyde and CO ₂ ;
Glycolaldehyde dehydrogenase (EC No. 1.2.40) catalyzing a chemical reaction that metabolizes Glycolaldehyde, NAD +, and H ₂ O produced by catalyzing the hydroxypyruvate decarboxylase (EC No. 4.1.1.40) to Glycolate, NADH, h, and h. 1.21),
Glycolate dehydrogenase (EC number 1.1.99.14) catalyzing a chemical reaction of metabolizing Glycolate and Acceptor produced by catalyzing the glycolaldehyde dehydrogenase (EC number 1.2.1.21) to Glyoxylate and Reduced acceptor;
Malate synthase (EC number 2.3) that catalyzes a chemical reaction that metabolizes Glyoxylate, Acetyl-CoA, and H ₂ O catalyzed by the glycolate dehydrogenase (EC number 1.1.99.14) to (S) -Malate and CoA. .3.9)
Malate dehydrogenase (EC number 1.1.1.40) catalyzing the chemical reaction of metabolizing (S) -Malate and NADP + produced by catalysed by the malate synthase (EC number 2.3.3.9) to Pyruvate, CO ₂ and NADPH The enzyme network according to claim 3, comprising: The third enzyme network is:
Catalyze a chemical reaction that metabolizes Pyruvate, CoA, and NADP + produced by catalyzing the 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14) to Acetyl-CoA, CO ₂ , and NADPH The enzyme network according to claim 4, further comprising pyruvate dehydrogenase (EC number 1.2.1.51). The third enzyme network is:
Phosphoglycerate mutase (EC number) catalyzing a chemical reaction that metabolizes 3-Phospho-D-glycerate produced by catalyzing the glyceraldehyde-3-phosphate dehydrogenase (EC number 1.2.1.9) to 2-Phospho-D-glycerate 5.4.2.1)
Phosphopyruvate hydratase (EC number 4.2.1.11) that catalyzes a chemical reaction that metabolizes 2-Phospho-D-glycerate produced by catalyzing the phosphoglycerate mutase (EC number 5.4.2.1) to Phosphoenolpyruvate and H ₂ O;
The compound further comprises pyruvate kinase (EC number 2.7.1.40) that catalyzes a chemical reaction that metabolizes Phosphoenolpyruvate and ADP produced by catalyzing the phosphopyruvate hydratase (EC number 4.2.1.11) to ATP and Pyruvate. The described enzyme network. An enzyme fuel cell that uses the catalytic action of an enzyme to metabolize glucose (D-Glucose) into carbon dioxide (CO ₂ ) to generate electricity,
As an enzyme network consisting of a plurality of enzymes that catalyzes a series of chemical reactions that metabolize the glucose (D-Glucose) to the carbon dioxide (CO ₂ ).
A first enzyme network that catalyzes a series of chemical reactions that metabolize D-Glucose to 6-Phospho-D-gluconate;
Phosphogluconate catalyzing a chemical reaction in which 6-Phospho-D-gluconate produced by catalysis by the first enzyme network is metabolized to 2-Dehydro-3-deoxy-6-phospho-D-gluconate and H ₂ O dehydratase (EC number 4.2.1.12),
2-Dehydro-3-deoxy-6-phospho-D-gluconate produced by catalyzing the phosphogluconate dehydratase (EC No. 4.2.1.12) is converted into Pyruvate and (2R) -2-Hydroxy-3- (phosphonooxy)- 2-dehydro-3-deoxy-phosphogluconate aldolase (EC number 4.1.2.14) catalyzing the chemical reaction metabolized to propanal,
The 2-dehydro-3-deoxy- phosphogluconate aldolase (EC number 4.1.2.14) Pyruvate produced is catalyzed and (2R) -2-Hydroxy-3- second to metabolize (phosphonooxy) -propanal to CO ₂ An enzyme fuel cell comprising:

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