New enzymatic method of chiral amino acid synthesis by dynamic kinetic resolution of amino acid amides: use of stereoselective amino acid amidases in the presence of alpha-amino-epsilon-caprolactam racemase.
D- and L-amino acids were produced from L- and D-amino acid amides by D-aminopeptidase from Ochrobactrum anthropi C1-38 and L-amino acid amidase from Pseudomonas azotoformans IAM 1603, respectively, in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae as the catalyst by dynamic kinetic resolution of amino acid amides.
Yamaguchi
Shigenori
S
Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan.
Komeda
Hidenobu
H
Asano
Yasuhisa
Y
D042402:Achromobacter / Q000201:enzymology; D000577:Amides / Q000737:chemistry / Q000378:metabolism*; D000581:Amidohydrolases / Q000378:metabolism*; D000591:Amino Acid Isomerases / Q000378:metabolism*; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism*; D000626:Aminopeptidases / Q000378:metabolism; D007700:Kinetics; D015394:Molecular Structure; D020621:Ochrobactrum anthropi / Q000201:enzymology; D011549:Pseudomonas / Q000201:enzymology; D013237:Stereoisomerism; D013696:Temperature
D000577:Amides; D000596:Amino Acids; D000626:Aminopeptidases; D000581:Amidohydrolases; D000591:Amino Acid Isomerases; C036861:aminocaprolactam racemase