DEACETYLATION OF PS-5, A NEW β-LACTAM COMPOUND
III. ENZYMOLOGICAL CHARACTERIZATION OF L-AMINO ACID ACYLASE AND D-AMINO ACID ACYLASE FROM PSEUDOMONAS SP. 1158
1980 Volume 33 Issue 6 Pages 556-565
Details
1980 Volume 33 Issue 6 Pages 556-565
L-Amino acid acylase and D-amino acid acylase were stable below 50°C, although the D-enzyme was more thermostable than the L-enzyme at higher temperatures. At 30°C they Showed the highest reaction velocity in phosphate buffer of pH 7.4. Hg++ and Cu++ severely inactivated their activity. Activation by Co++ was observed on L-amino acid acylase, but not on D-amino acid acylase. p-Chloromercuribenzoate inhibited both enzymes, whereas ethylenediamine tetraacetate was very inhibitory on L-amino acid acylase only. With N-acetyl- and
N-chloroacetyl-aminao aids as substrates, they were relatively stereo-specific. They acted as a Peptidase on dipeptides and tripeptides. Although N-acetylglycine wes attacked by the two enzymes, N-acetylglucosamine and N-acetylethanolamine were insusceptible. PS-5 was converted to NS-5 (deacetyl PS-5) by L-amino acid acylase as well as by D-amino acid acylase.
