Deracemization of Phenyl‐Substituted 2‐Methyl‐1,2,3,4‐Tetrahydroquinolines by a Recombinant Monoamine Oxidase from  Pseudomonas monteilii  ZMU‐T01 | Zendy

Deng Guozhong | Zendy; Wan Nanwei | Zendy; Qin Lei | Zendy; Cui Baodong | Zendy; An Miao | Zendy; Han Wenyong | Zendy; Chen Yongzheng | Zendy

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Deracemization of Phenyl‐Substituted 2‐Methyl‐1,2,3,4‐Tetrahydroquinolines by a Recombinant Monoamine Oxidase from Pseudomonas monteilii ZMU‐T01

Author(s) -

Deng Guozhong,

Wan Nanwei,

Qin Lei,

Cui Baodong,

An Miao,

Han Wenyong,

Chen Yongzheng

Publication year - 2018

Publication title -

chemcatchem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.497

H-Index - 106

eISSN - 1867-3899

pISSN - 1867-3880

DOI - 10.1002/cctc.201701995

Subject(s) - pseudomonas , monoamine oxidase , chemistry , biocatalysis , enantiomer , enantiomeric excess , escherichia coli , recombinant dna , oxidase test , stereochemistry , monoamine neurotransmitter , biochemistry , enzyme , enantioselective synthesis , organic chemistry , biology , catalysis , bacteria , serotonin , gene , reaction mechanism , genetics , receptor

A monoamine oxidase (MAO5) from Pseudomonas monteilii ZMU‐T01 was first heterologously expressed in Escherichia coli BL21(DE3) and then used as a biocatalyst for the deracemization of racemic 2‐methyl‐1,2,3,4‐tetrahdroquinoline derivatives to yield the unreacted R enantiomer with up to >99 % ee . Sequence alignment revealed that MAO5 shared 14.7 % identity toward the well‐studied monoamine oxidase (MAO‐N).

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