Literature DB >> 23584786

ω-Transaminase from Ochrobactrum anthropi is devoid of substrate and product inhibitions.

Eul-Soo Park1, Jong-Shik Shin.   

Abstract

ω-Transaminases display complicated inhibitions by ketone products and both enantiomers of amine substrates. Here, we report the first example of ω-transaminase devoid of such inhibitions. Owing to the lack of enzyme inhibitions, the ω-transaminase from Ochrobactrum anthropi enabled efficient kinetic resolution of α-methylbenzylamine (500 mM) even without product removal.

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Year:  2013        PMID： 23584786      PMCID： PMC3697560          DOI： 10.1128/AEM.03811-12

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN： 0099-2240            Impact factor:   4.792


  16 in total

Review 1.  omega-Transaminases for the synthesis of non-racemic alpha-chiral primary amines.

Authors:  Dominik Koszelewski; Katharina Tauber; Kurt Faber; Wolfgang Kroutil
Journal:  Trends Biotechnol       Date:  2010-04-27       Impact factor: 19.536

2.  Efficient asymmetric synthesis of chiral amines by combining transaminase and pyruvate decarboxylase.

Authors:  Matthias Höhne; Steffen Kühl; Karen Robins; Uwe T Bornscheuer
Journal:  Chembiochem       Date:  2008-02-15       Impact factor: 3.164

3.  Efficient kinetic resolution of racemic amines using a transaminase in combination with an amino acid oxidase.

Authors:  Matthew D Truppo; Nicholas J Turner; J David Rozzell
Journal:  Chem Commun (Camb)       Date:  2009-03-16       Impact factor: 6.222

4.  Molecular determinants for substrate selectivity of ω-transaminases.

Authors:  Eul-Soo Park; Minji Kim; Jong-Shik Shin
Journal:  Appl Microbiol Biotechnol       Date:  2011-10-09       Impact factor: 4.813

5.  Kinetic modeling of omega-transamination for enzymatic kinetic resolution of alpha-methylbenzylamine.

Authors:  J S Shin; B G Kim
Journal:  Biotechnol Bioeng       Date:  1998-12-05       Impact factor: 4.530

6.  Kinetic resolution of chiral amines with omega-transaminase using an enzyme-membrane reactor.

Authors:  J S Shin; B G Kim; A Liese; C Wandrey
Journal:  Biotechnol Bioeng       Date:  2001-05-05       Impact factor: 4.530

7.  Comparison of the omega-transaminases from different microorganisms and application to production of chiral amines.

Authors:  J S Shin; B G Kim
Journal:  Biosci Biotechnol Biochem       Date:  2001-08       Impact factor: 2.043

Review 8.  Features and technical applications of ω-transaminases.

Authors:  M Shaheer Malik; Eul-Soo Park; Jong-Shik Shin
Journal:  Appl Microbiol Biotechnol       Date:  2012-05-04       Impact factor: 4.813

9.  Substrate inhibition mode of omega-transaminase from Vibrio fluvialis JS17 is dependent on the chirality of substrate.

Authors:  Jong-Shik Shin; Byung-Gee Kim
Journal:  Biotechnol Bioeng       Date:  2002-03-30       Impact factor: 4.530

Review 10.  Novel biosynthetic approaches to the production of unnatural amino acids using transaminases.

Authors:  P P Taylor; D P Pantaleone; R F Senkpeil; I G Fotheringham
Journal:  Trends Biotechnol       Date:  1998-10       Impact factor: 19.536
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  3 in total

1.  Improvement of whole-cell transamination with Saccharomyces cerevisiae using metabolic engineering and cell pre-adaptation.

Authors:  Nora Weber; Marie Gorwa-Grauslund; Magnus Carlquist
Journal:  Microb Cell Fact       Date:  2017-01-03       Impact factor: 5.328

2.  Exploiting cell metabolism for biocatalytic whole-cell transamination by recombinant Saccharomyces cerevisiae.

Authors:  Nora Weber; Marie Gorwa-Grauslund; Magnus Carlquist
Journal:  Appl Microbiol Biotechnol       Date:  2014-02-21       Impact factor: 4.813

3.  Structural studies reveal flexible roof of active site responsible for ω-transaminase CrmG overcoming by-product inhibition.

Authors:  Jinxin Xu; Xiaowen Tang; Yiguang Zhu; Zhijun Yu; Kai Su; Yulong Zhang; Yan Dong; Weiming Zhu; Changsheng Zhang; Ruibo Wu; Jinsong Liu
Journal:  Commun Biol       Date:  2020-08-19
  3 in total

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