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ω-Transaminase from Ochrobactrum anthropi is devoid of substrate and product inhibitions.
Park, Eul-Soo; Shin, Jong-Shik.
Affiliation
  • Park ES; Department of Biotechnology, Yonsei University, Seoul, South Korea.
Appl Environ Microbiol ; 79(13): 4141-4, 2013 Jul.
Article in En | MEDLINE | ID: mdl-23584786
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phenethylamines / Ochrobactrum anthropi / Enzyme Inhibitors / Transaminases Language: En Journal: Appl Environ Microbiol Year: 2013 Document type: Article Affiliation country: Korea (South) Country of publication: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phenethylamines / Ochrobactrum anthropi / Enzyme Inhibitors / Transaminases Language: En Journal: Appl Environ Microbiol Year: 2013 Document type: Article Affiliation country: Korea (South) Country of publication: United States