D-Aminoacylase from Alcaligenes faecalis possesses novel activities on D-methionine.
D-Aminoacylase isolated from Alcaligenes faecalis DA1 has a great potential for future application in D-amino acids production. This paper reports for the first time that D-aminoacylase can reverse the catalysis direction on D-Met and deacylate N-Ac-D-Met-OMe and N-Ac-D-Met-Gly. The results provide important insights regarding the binding and affinity of substrates to the active site of this enzyme. Based on a systematic study of kinetic properties and relative reactivities for a broad range of substrates, a model to elucidate the reaction mechanism is proposed.
Chen
H P
HP
Department of Biochemistry, China Medical College, Taichung, Taiwan.
Wu
S H
SH
Wang
K T
KT
D000215:Acylation; D000421:Alcaligenes / Q000201:enzymology*; D000581:Amidohydrolases / Q000378:metabolism*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D004151:Dipeptides / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D008715:Methionine / Q000737:chemistry / Q000378:metabolism*; D008956:Models, Chemical; D015394:Molecular Structure; D013237:Stereoisomerism; D013379:Substrate Specificity
D000596:Amino Acids; D004151:Dipeptides; D008715:Methionine; D000581:Amidohydrolases; C019672:aminoacylase I