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

Eul Soo Park; Jong Shik Shin

doi:10.1128/AEM.03811-12

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

Eul Soo Park, Jong Shik Shin

Research output: Contribution to journal › Article › peer-review

26 Citations (Scopus)

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.

Original language	English
Pages (from-to)	4141-4144
Number of pages	4
Journal	Applied and Environmental Microbiology
Volume	79
Issue number	13
DOIs	https://doi.org/10.1128/AEM.03811-12
Publication status	Published - 2013 Jul

All Science Journal Classification (ASJC) codes

Biotechnology
Food Science
Applied Microbiology and Biotechnology
Ecology

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

Abstract

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