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

Eul Soo Park, jong shik shin

Research output: Contribution to journalArticle

17 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 languageEnglish
Pages (from-to)4141-4144
Number of pages4
JournalApplied and Environmental Microbiology
Volume79
Issue number13
DOIs
Publication statusPublished - 2013 Jul 1

Fingerprint

Ochrobactrum anthropi
transaminases
Transaminases
substrate
enzyme inhibition
enantiomers
ketone
ketones
Ketones
amines
Amines
enzyme
kinetics
Enzymes
product

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

Cite this

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ω-Transaminase from Ochrobactrum anthropi is devoid of substrate and product inhibitions. / Park, Eul Soo; shin, jong shik.

In: Applied and Environmental Microbiology, Vol. 79, No. 13, 01.07.2013, p. 4141-4144.

Research output: Contribution to journalArticle

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