Stereochemistry of 2-phenylethylamine oxidation catalyzed by bacterial copper amine oxidase.
The stereochemical course of the reaction catalyzed by a copper amine oxidase from Arthrobacter globiformis has been investigated using 2-phenylethylamine stereospecifically deuterium-labeled at the C1 position. Measurements of deuterium content in the product, phenylacetaldehyde, by gas chromatography-mass spectrometry revealed stereospecific abstraction of the pro-S hydrogen during the enzymatic oxidation, as predicted from the structure modeling for the enzyme-bound substrate.
Uchida
Mayumi
M
Graduate School of Human and Environmental Studies, Kyoto University, Japan.
Ohtani
Akifumi
A
Kohyama
Naoki
N
Okajima
Toshihide
T
Tanizawa
Katsuyuki
K
Yamamoto
Yukio
Y
D000079:Acetaldehyde / Q000031:analogs & derivatives* / Q000737:chemistry*; D006631:Amine Oxidase (Copper-Containing) / Q000378:metabolism*; D002849:Chromatography, Gas; D003903:Deuterium / Q000737:chemistry*; D013058:Mass Spectrometry; D008835:Micrococcaceae / Q000201:enzymology; D008968:Molecular Conformation; D010084:Oxidation-Reduction; D010627:Phenethylamines / Q000737:chemistry*; D013237:Stereoisomerism
D010627:Phenethylamines; C029261:phenethylamine; D003903:Deuterium; D006631:Amine Oxidase (Copper-Containing); D000079:Acetaldehyde; C013192:phenylacetaldehyde