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

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

SUBMITTER: Park ES

PROVIDER: S-EPMC3697560 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature

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

Park Eul-Soo ES Shin Jong-Shik JS

Applied and environmental microbiology 20130412 13

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. ...[more]

PMID: 23584786

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2016-12-13 | PXD004654 | Pride

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