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

Appl Environ Microbiol. 2013 Jul;79(13):4141-4. doi: 10.1128/AEM.03811-12. Epub 2013 Apr 12.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Inhibitors / metabolism*
  • Kinetics
  • Molecular Structure
  • Ochrobactrum anthropi / enzymology*
  • Phenethylamines / metabolism*
  • Transaminases / chemistry
  • Transaminases / metabolism*

Substances

  • Enzyme Inhibitors
  • Phenethylamines
  • Transaminases
  • 1-phenethylamine