Deacetylation of PS-5, a new .BETA.-lactam compound. III. Enzymological characterization of L-amino acid acylase and D-amino acid acylase from Pseudomonas sp. 1158.

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Abstract
L- and D-Amino acid acylases were stable below 50.degree. C, although the D-enzyme was more thermostable than the L-enzyme at higher temperatures. At 30.degree. C they showed the highest reaction velocity in phosphate buffer of pH 7.4. Hg2+ and Cu2+ severely inactivated their activity. Activation by Co2+ was observed on L-amino acid acylase, but not on D-amino acid acylase. p-Chloromercuribenzoate inhibited both enzymes, whereas EDTA was very inhibitory on L-amino acid acylase only. With N-acetyl- and N-chloroacetyl-amino acids as substrates, they were relatively stereo-specific. They acted as a peptidase on dipeptides and tripeptides. Although N-acetylglycine was attacked by the 2 enzymes, N-acetylglucosamine and N-acetylethanolamine were unsusceptible. PS 5 was converted to NS 5 (deacetyl PS 5) by L- and by D-amino acid acylases.

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