AR098490A1 - MUTANTS OF THE GEN CODIFYING THE ENZYME PHENYLACETONE MONOOXIGENASA (PAMO) - Google Patents

MUTANTS OF THE GEN CODIFYING THE ENZYME PHENYLACETONE MONOOXIGENASA (PAMO)

Info

Publication number
AR098490A1
AR098490A1 ARP140104366A ARP140104366A AR098490A1 AR 098490 A1 AR098490 A1 AR 098490A1 AR P140104366 A ARP140104366 A AR P140104366A AR P140104366 A ARP140104366 A AR P140104366A AR 098490 A1 AR098490 A1 AR 098490A1
Authority
AR
Argentina
Prior art keywords
pamo
mutants
enzyme
phenylacetone
caprolactone
Prior art date
Application number
ARP140104366A
Other languages
Spanish (es)
Original Assignee
Pontificia Univ Católica De Chile
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Pontificia Univ Católica De Chile filed Critical Pontificia Univ Católica De Chile
Publication of AR098490A1 publication Critical patent/AR098490A1/en

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y114/00—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14)
    • C12Y114/13—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14) with NADH or NADPH as one donor, and incorporation of one atom of oxygen (1.14.13)
    • C12Y114/13092—Phenylacetone monooxygenase (1.14.13.92)
    • 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.)
    • C12N9/0071—Oxidoreductases (1.) acting on paired donors with incorporation of molecular oxygen (1.14)
    • C12N9/0073—Oxidoreductases (1.) acting on paired donors with incorporation of molecular oxygen (1.14) with NADH or NADPH as one donor, and incorporation of one atom of oxygen 1.14.13
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P17/00—Preparation of heterocyclic carbon compounds with only O, N, S, Se or Te as ring hetero atoms
    • C12P17/02—Oxygen as only ring hetero atoms
    • C12P17/08—Oxygen as only ring hetero atoms containing a hetero ring of at least seven ring members, e.g. zearalenone, macrolide aglycons
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P7/00—Preparation of oxygen-containing organic compounds
    • C12P7/62—Carboxylic acid esters

Landscapes

  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Health & Medical Sciences (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Genetics & Genomics (AREA)
  • General Health & Medical Sciences (AREA)
  • General Engineering & Computer Science (AREA)
  • Biochemistry (AREA)
  • Biotechnology (AREA)
  • Microbiology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Medicinal Chemistry (AREA)
  • Molecular Biology (AREA)
  • Biomedical Technology (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

La presente se refiere a mutantes del gen que codifica para la enzima fenilacetona monooxigenasa (PAMO) que fue aislada a partir de la bacteria de nombre científico Thermofibida fusca o Thermomonospora fusca con sustituciones en las posiciones 93, 94 y 440 (N, D y F, respectivamente) de la secuencia original de amino ácidos, y combinaciones de sustituciones especificas de las posiciones 441, 442, 443 y/o 444 (G o D, P o E, T, V, I o W y Q, respectivamente), las que muestran tanto un alto rendimiento como catalizadores en la conversión de ciclohexanona a e-caprolactona, como también alta estabilidad térmica. ADN codificante para dichas enzimas y secuencias, amino acídicas codificadas, las cuales se proponen como biocatalizadores para un proceso de conversión más eficiente y con menor generación de residuos tóxicos comparado con los procesos industriales existentes de producción de e-caprolactona.This refers to mutants of the gene encoding the enzyme phenylacetone monooxygenase (PAMO) that was isolated from the bacterium of scientific name Thermofibida fusca or Thermomonospora fusca with substitutions at positions 93, 94 and 440 (N, D and F , respectively) of the original amino acid sequence, and combinations of specific substitutions at positions 441, 442, 443 and / or 444 (G or D, P or E, T, V, I or W and Q, respectively), those that show both high performance and catalysts in the conversion of cyclohexanone to e-caprolactone, as well as high thermal stability. DNA coding for said enzymes and sequences, amino acid codified amino acids, which are proposed as biocatalysts for a more efficient conversion process and with less generation of toxic waste compared to the existing industrial processes of production of e-caprolactone.

ARP140104366A 2013-11-22 2014-11-20 MUTANTS OF THE GEN CODIFYING THE ENZYME PHENYLACETONE MONOOXIGENASA (PAMO) AR098490A1 (en)

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
CL2013003356A CL2013003356A1 (en) 2013-11-22 2013-11-22 Mutants of the gene coding for the phenylacetone monooxygenase (pamo) enzyme isolated from fusca or thermononospora fusca thermofibide with substitutions at positions 93.94, and 440 (n, dyf, respectively) and specific combinations of positions 441,442,443 and / or 444 (god , poe, t, v, iowyq respectively) with high performance as catalysts in the conversion of cyclohexanone to epailon-caprolactone and high thermal stability, DNA conditioning and encoded amino acidic sequences.

Publications (1)

Publication Number Publication Date
AR098490A1 true AR098490A1 (en) 2016-06-01

Family

ID=53178765

Family Applications (1)

Application Number Title Priority Date Filing Date
ARP140104366A AR098490A1 (en) 2013-11-22 2014-11-20 MUTANTS OF THE GEN CODIFYING THE ENZYME PHENYLACETONE MONOOXIGENASA (PAMO)

Country Status (3)

Country Link
AR (1) AR098490A1 (en)
CL (1) CL2013003356A1 (en)
WO (1) WO2015074162A1 (en)

Families Citing this family (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN113430216B (en) * 2021-07-26 2023-07-21 福州大学 Propiophenone monooxygenase and application thereof in preparing azole medicines
CN115927220A (en) * 2022-08-30 2023-04-07 凯莱英医药集团（天津）股份有限公司 Monooxygenase mutants and application thereof

Family Cites Families (18)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0728197A1 (en) 1993-11-05 1996-08-28 Cornell Research Foundation, Inc. THERMOSTABLE XYLANASE FROM A $i(THERMOMONOSPORA FUSCA) GENE
US5677151A (en) 1994-06-24 1997-10-14 Cornell Research Foundation, Inc. Thermostable cellulase from a thermomonospora gene
US5871550A (en) 1997-08-26 1999-02-16 Genencor International, Inc. Mutant Thermonospora spp. cellulase
US6365376B1 (en) 1999-02-19 2002-04-02 E. I. Du Pont De Nemours And Company Genes and enzymes for the production of adipic acid intermediates
DE50014445D1 (en) 1999-09-30 2007-08-09 Biotechnolog Forschung Gmbh ESTERGROUP COLUMN ENZYM FROM THERMOMONOSPORA FUSCA
DE60034303T2 (en) 2000-01-31 2008-01-03 Solvay (Société Anonyme) A method of oxidation with a catalyst of an antimony trifluoride and silica containing composition
ES2254402T3 (en) 2000-08-24 2006-06-16 UNION CARBIDE CHEMICALS & PLASTICS TECHNOLOGY CORPORATION PROCEDURES FOR THE MANUFACTURE OF LACTONS.
US7105296B2 (en) 2001-08-29 2006-09-12 E. I. Du Pont De Nemours And Company Genes encoding Baeyer-Villiger monooxygenases
DE10308489A1 (en) 2003-02-26 2004-09-09 Basf Ag Process for the preparation of cyclopentanone and caprolactone from dicarboxylic acid solution
JP2008247889A (en) 2007-03-05 2008-10-16 Sumitomo Chemical Co Ltd PRODUCTION METHOD OF epsilon-CAPROLACTONE COMPOUND
US7666751B2 (en) 2007-09-21 2010-02-23 Semiconductor Components Industries, Llc Method of forming a high capacitance diode and structure therefor
CN102260655B (en) 2009-12-18 2012-07-25 江南大学 Cutinase mutants and preparation method thereof
CN102260634B (en) 2010-05-28 2012-11-21 中国科学院成都生物研究所 High-efficiency formaldehyde degrading bacteria and use and using method thereof
WO2011159551A1 (en) 2010-06-16 2011-12-22 Bioamber S.A.S. Processes for the production of hydrogenated products and derivatives thereof
EP2614056B1 (en) 2010-09-08 2014-07-23 Basf Se Methods for the production of epsilon-caprolactone and 1,6-hexanediol
EP2636665B1 (en) 2010-11-02 2016-06-22 National University Corporation Nagoya University Method for producing ester
MY171760A (en) 2011-11-02 2019-10-28 Genomatica Inc Microorganisms and methods for the production of caprolactone
CN102443578B (en) 2011-12-08 2013-10-16 江南大学 Glucose isomerase mutant and application thereof

Also Published As

Publication number Publication date
CL2013003356A1 (en) 2014-08-08
WO2015074162A1 (en) 2015-05-28

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