Hydrolysis of N-phenylacetyl-a-methyl-alpha-amino acids by benzylpenicillinacylase.
Enzymatic hydrolysis of several racemic N-phenylacetyl-alpha-methyl-alpha-amino acids containing an additional aliphatic, aromatic or polar substitutent on the chiral carbon atom, has been studied by using benzylpenicillinacylase from Escherichia coli A.T.C.C.9637. Both the rate of hydrolysis and the stereoselectivity were found to be considerably lower than in the case of natural alpha-amino acids. Steric and electronic factors in the side chains influencing the stereoselectivity are discussed. Key words. Benzylpenicillinacylase; enzymatic hydrolysis; alpha-methyl-alpha-amino acids.
D000581:Amidohydrolases / Q000378:metabolism*; D000596:Amino Acids / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D006868:Hydrolysis; D010399:Penicillin Amidase / Q000378:metabolism*; D010648:Phenylacetates / Q000378:metabolism; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D000596:Amino Acids; D010648:Phenylacetates; D000581:Amidohydrolases; D010399:Penicillin Amidase