Inversion of enantioselectivity of asymmetric biocatalytic decarboxylation by site-directed mutagenesis based on the reaction mechanism.
The introduction of two mutations (G74C/C188S) based on the estimated reaction mechanism resulted in the inversion of enantioselectivity of arylmalonate decarboxylase, which catalyses the asymmetric decarboxylation of arylmethylmalonate to give optically active arylpropionate.
Ijima
Yoichiro
Y
Department of Biosciences and Informatics, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.
Matoishi
Kaori
K
Terao
Yosuke
Y
Doi
Nobuhide
N
Yanagawa
Hiroshi
H
Ohta
Hiromichi
H
D000595:Amino Acid Sequence; D002262:Carboxy-Lyases / Q000737:chemistry* / Q000235:genetics*; D002384:Catalysis; D003653:Decarboxylation; D008764:Methylmalonic Acid / Q000737:chemistry*; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011422:Propionates / Q000138:chemical synthesis*; D013237:Stereoisomerism
D011422:Propionates; D008764:Methylmalonic Acid; D002262:Carboxy-Lyases; C071852:malonate decarboxylase