DE102008030435A1 - Neuartige Varianten PQQ-abhängiger Glukosehydrogenase mit verbesserter Substratspezifität - Google Patents
Neuartige Varianten PQQ-abhängiger Glukosehydrogenase mit verbesserter Substratspezifität Download PDFInfo
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- DE102008030435A1 DE102008030435A1 DE102008030435A DE102008030435A DE102008030435A1 DE 102008030435 A1 DE102008030435 A1 DE 102008030435A1 DE 102008030435 A DE102008030435 A DE 102008030435A DE 102008030435 A DE102008030435 A DE 102008030435A DE 102008030435 A1 DE102008030435 A1 DE 102008030435A1
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- spqqgdh
- glucose
- amino acids
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- enzyme
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/001—Enzyme electrodes
- C12Q1/005—Enzyme electrodes involving specific analytes or enzymes
- C12Q1/006—Enzyme electrodes involving specific analytes or enzymes for glucose
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/26—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase
- C12Q1/32—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase involving dehydrogenase
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01069—Gluconate 5-dehydrogenase (1.1.1.69)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/05—Oxidoreductases acting on the CH-OH group of donors (1.1) with a quinone or similar compound as acceptor (1.1.5)
- C12Y101/05002—Quinoprotein glucose dehydrogenase (1.1.5.2)
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Analytical Chemistry (AREA)
- Immunology (AREA)
- Physics & Mathematics (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- Emergency Medicine (AREA)
- Enzymes And Modification Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Apparatus Associated With Microorganisms And Enzymes (AREA)
Priority Applications (7)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE102008030435A DE102008030435A1 (de) | 2008-06-26 | 2008-06-26 | Neuartige Varianten PQQ-abhängiger Glukosehydrogenase mit verbesserter Substratspezifität |
| CN201310472347.1A CN103540572A (zh) | 2008-06-26 | 2009-06-17 | 具有改善的底物特异性的pqq-依赖性葡萄糖脱氢酶的新变体 |
| PCT/EP2009/004350 WO2009156083A1 (de) | 2008-06-26 | 2009-06-17 | Neuartige varianten pqq-abhängiger glukosedehydrogenase mit verbesserter substratspezifität |
| US12/999,465 US8580547B2 (en) | 2008-06-26 | 2009-06-17 | Variants of PQQ-dependent glucose dehydrogenase having improved substrate specificity |
| JP2011515164A JP2011525361A (ja) | 2008-06-26 | 2009-06-17 | 向上した基質特異性を有するｐｑｑ−依存的グルコースデヒドロゲナーゼの新規変異体 |
| CN200980124063.5A CN102076846A (zh) | 2008-06-26 | 2009-06-17 | 具有改善的底物特异性的pqq-依赖性葡萄糖脱氢酶的新变体 |
| EP09768932A EP2294188A1 (de) | 2008-06-26 | 2009-06-17 | Neuartige varianten pqq-abhängiger glukosedehydrogenase mit verbesserter substratspezifität |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE102008030435A DE102008030435A1 (de) | 2008-06-26 | 2008-06-26 | Neuartige Varianten PQQ-abhängiger Glukosehydrogenase mit verbesserter Substratspezifität |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| DE102008030435A1 true DE102008030435A1 (de) | 2010-01-07 |
Family
ID=40972803
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DE102008030435A Withdrawn DE102008030435A1 (de) | 2008-06-26 | 2008-06-26 | Neuartige Varianten PQQ-abhängiger Glukosehydrogenase mit verbesserter Substratspezifität |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US8580547B2 (https=) |
| EP (1) | EP2294188A1 (https=) |
| JP (1) | JP2011525361A (https=) |
| CN (2) | CN102076846A (https=) |
| DE (1) | DE102008030435A1 (https=) |
| WO (1) | WO2009156083A1 (https=) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU2011355209B2 (en) | 2010-12-20 | 2015-09-17 | Lek Pharmaceuticals D.D. | Enzymatic synthesis of active pharmaceutical ingredient and intermediates thereof |
| EP2465936A1 (en) | 2010-12-20 | 2012-06-20 | LEK Pharmaceuticals d.d. | Enzymatic synthesis of statins and intermediates thereof |
| CN105331591B (zh) | 2015-10-29 | 2020-02-28 | 英科隆生物技术（杭州）有限公司 | PQQ-sGDH突变体、聚核苷酸及葡萄糖检测装置 |
| CN109085269B (zh) * | 2018-08-15 | 2021-03-09 | 江苏省原子医学研究所 | PQQ与Lys及Arg反应行为研究的方法 |
Citations (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1146332A1 (en) | 1999-10-05 | 2001-10-17 | Matsushita Electric Industrial Co., Ltd. | Glucose sensor |
| EP1367120A2 (en) | 2002-05-27 | 2003-12-03 | Toyo Boseki Kabushiki Kaisha | Modified pyrroloquinoline quinone (PQQ) dependent glucose dehydrogenase with superior substrate specificity and stability |
| EP1623025A1 (de) | 2003-05-07 | 2006-02-08 | Bayer Technology Services GmbH | Glukose dehydrogenase und ihre herstellung |
| EP1666586A1 (en) | 2003-09-08 | 2006-06-07 | Toyo Boseki Kabushiki Kaisha | Pyrroloquinoline quinone (pqq)-dependent glucose dehydrogenase modification having excellent substrate specificity |
| WO2006085509A1 (ja) * | 2005-02-08 | 2006-08-17 | Toyo Boseki Kabushiki Kaisha | 基質特異性に優れた改変型ピロロキノリンキノン依存性グルコースデヒドロゲナーゼ |
| JP2006217810A (ja) * | 2005-02-08 | 2006-08-24 | Toyobo Co Ltd | 基質特異性に優れたピロロキノリンキノン（ｐｑｑ）依存性グルコースデヒドロゲナーゼ改変体 |
| US7132270B2 (en) | 2000-10-27 | 2006-11-07 | Roche Diagnostics Gmbh | Forms of soluble pyrroloquinoline quinone-dependent glucose dehydrogenase |
| JP2007000020A (ja) * | 2005-06-21 | 2007-01-11 | Toyobo Co Ltd | 基質特異性に優れたピロロキノリンキノン（ｐｑｑ）依存性グルコースデヒドロゲナーゼ改変体 |
| JP2007043983A (ja) * | 2005-08-11 | 2007-02-22 | Toyobo Co Ltd | 基質特異性に優れた改変型ピロロキノリンキノン依存性グルコースデヒドロゲナーゼ |
-
2008
- 2008-06-26 DE DE102008030435A patent/DE102008030435A1/de not_active Withdrawn
-
2009
- 2009-06-17 EP EP09768932A patent/EP2294188A1/de not_active Withdrawn
- 2009-06-17 CN CN200980124063.5A patent/CN102076846A/zh active Pending
- 2009-06-17 US US12/999,465 patent/US8580547B2/en not_active Expired - Fee Related
- 2009-06-17 JP JP2011515164A patent/JP2011525361A/ja active Pending
- 2009-06-17 CN CN201310472347.1A patent/CN103540572A/zh active Pending
- 2009-06-17 WO PCT/EP2009/004350 patent/WO2009156083A1/de not_active Ceased
Patent Citations (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1146332A1 (en) | 1999-10-05 | 2001-10-17 | Matsushita Electric Industrial Co., Ltd. | Glucose sensor |
| US7132270B2 (en) | 2000-10-27 | 2006-11-07 | Roche Diagnostics Gmbh | Forms of soluble pyrroloquinoline quinone-dependent glucose dehydrogenase |
| EP1367120A2 (en) | 2002-05-27 | 2003-12-03 | Toyo Boseki Kabushiki Kaisha | Modified pyrroloquinoline quinone (PQQ) dependent glucose dehydrogenase with superior substrate specificity and stability |
| EP1623025A1 (de) | 2003-05-07 | 2006-02-08 | Bayer Technology Services GmbH | Glukose dehydrogenase und ihre herstellung |
| EP1666586A1 (en) | 2003-09-08 | 2006-06-07 | Toyo Boseki Kabushiki Kaisha | Pyrroloquinoline quinone (pqq)-dependent glucose dehydrogenase modification having excellent substrate specificity |
| WO2006085509A1 (ja) * | 2005-02-08 | 2006-08-17 | Toyo Boseki Kabushiki Kaisha | 基質特異性に優れた改変型ピロロキノリンキノン依存性グルコースデヒドロゲナーゼ |
| JP2006217810A (ja) * | 2005-02-08 | 2006-08-24 | Toyobo Co Ltd | 基質特異性に優れたピロロキノリンキノン（ｐｑｑ）依存性グルコースデヒドロゲナーゼ改変体 |
| JP2007000020A (ja) * | 2005-06-21 | 2007-01-11 | Toyobo Co Ltd | 基質特異性に優れたピロロキノリンキノン（ｐｑｑ）依存性グルコースデヒドロゲナーゼ改変体 |
| JP2007043983A (ja) * | 2005-08-11 | 2007-02-22 | Toyobo Co Ltd | 基質特異性に優れた改変型ピロロキノリンキノン依存性グルコースデヒドロゲナーゼ |
Non-Patent Citations (18)
| Title |
|---|
| A. M Cleton-Jansen et al., J. Bacteriol. 170 [5], 2121-2125 (1988) |
| A. M Cleton-Jansen et al., Mol. Gen. Genet. 217 [2-3], 430-436 (1989) |
| A. Oubrie et al., J. Mol. Biol. 289 [2], 319-333 (1999); A. Oubrie et al., EMBO J. 18 [19], 5187-5194 (1999) |
| H. E. Pauly und G. Pfleiderer, Hoppe Seglers. Z. Physiol Chem. 356 [10], 1613-1623 (1975) |
| http://www.ncbi.nlm.nih.gov/Structure/CN3D/cn3d.shtml |
| Igarashi, S. [u.a.]: Engineering PQO glucose dehydrogenase with improved substrate specificity, Site directed mutagenesis studies on the active center of PQO glucose dehydrogenase, In. Biomolecular Engineering, 2004, Vol. 21, S. 81-89 * |
| K. Kojima K. et al., Biotechnology Letters 22, 1343-1347 (2000) |
| Molecular Cloning - A Laboratory Manual; Sambrook, J. und Russel, D. W.; 3. Auflage, CSHL Press 2001 |
| P. J. Bouvet P. J. und O. M. Bouvet, Res. Microbiol. 140 [8], 531-540 (1989) |
| P. Vadgama, J. Med. Eng Technol. 5 [6], 293-298 (1981), K. S. Chua und I. K. Tan, Clin. Chem. 24 [1], 150-152 (1978) |
| Pat. Abstr. of Jp. & JP 2006217810 A * |
| Pat. Abstr. of Jp. & JP 2007000020 A * |
| Pat. Abstr. of Jp. & JP 2007043983 A * |
| S. Igarashi et al., Biomol. Eng 21 [2], 81-89 (2004) |
| T. G. Schleis, Pharmacotherapy 27 [9], 1313-1321 (2007) |
| WO 2006085509 A1 mit den Familien JP 2007043983 A, JP 2007000020 A und JP 2006217810 A (jeweils Pat. Abstr. of Jp.) und den dazugehörigen übersetzten Patentansprüchen Igarashi, S. [u.a.]: Engineering PQO glucose dehydrogenase with improved substrate specificity, Site directed mutagenesis studies on the active center of PQO glucose dehydrogenase, In. Biomolecular Engineering, 2004, Vol. 21, S. 81-89 |
| z. B. Molecular Cloning - A Laboratory Manual; Vol. 1; Sambrook, J. und Russel, D. W., 3. Auflage, CSHL Press 2001 |
| z. B. Peter Atkins, Physical Chemistry, W. H. Freeman & Co; 7. Auflage, 2002 |
Also Published As
| Publication number | Publication date |
|---|---|
| CN102076846A (zh) | 2011-05-25 |
| US20110236920A1 (en) | 2011-09-29 |
| JP2011525361A (ja) | 2011-09-22 |
| EP2294188A1 (de) | 2011-03-16 |
| CN103540572A (zh) | 2014-01-29 |
| US8580547B2 (en) | 2013-11-12 |
| WO2009156083A1 (de) | 2009-12-30 |
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