title: ω-Transaminase from Ochrobactrum anthropi is devoid of substrate and product inhibitions.
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.
authors.affiliation: Department of Biotechnology, Yonsei University, Seoul, South Korea.
authors.forename: Eul-Soo
authors.initials: ES
authors.lastname: Park
authors.forename: Jong-Shik
authors.initials: JS
authors.lastname: Shin
mesh_terms: D004791:Enzyme Inhibitors / Q000378:metabolism*; D007700:Kinetics; D015394:Molecular Structure; D020621:Ochrobactrum anthropi / Q000201:enzymology*; D010627:Phenethylamines / Q000378:metabolism*; D000637:Transaminases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D004791:Enzyme Inhibitors; D010627:Phenethylamines; D000637:Transaminases; C033198:1-phenethylamine