Abstract
Enzymatic hydrolysis of several racemic N-phenylacetyl-α-methyl-α-amino acids containing an additinal aliphatic, aromatic or polar substitutent on the chiral carbon atom, has been studied by using benzylpenicillincylase fromEscherichia 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 α-amino acids. Steric and electronic factors in the side chains influencing the stereoselectivity are discussed.

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