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Polymyxin acylase from Pseudomonas sp. M-6-3 can deacylate not only polymyxin antibiotics, but also A-fatty acyl-peptides and N-fatty acyl-amino acids. We found that this enzyme causes intramolecular N2⇄N6 acyl transfer in monooctanoyl-l-lysine; when N2-octanoyl-l-lysine is the substrate, N6-octanoyl- l-lysine is produced at pH 10.5, but when N6-octanoyl- l-lysine is the substrate, N2-octanoyl- l-lysine is produced at pH 8.0. In these reactions, the deacylation proceeded gradually at the final stage and eventually, both N2-octanoyl- l-lysine and N6-octanoyl- l-lysine were hydrolyzed to l-lysine and octanoic acid. Furthermore, this enzyme showed intermolecular acyltrans- ferase activity, transferring several N-octanoyl- dl-amino acids to N-octanoyl-hydroxylamine. This acyltransfer ability of polymyxin acylase offers a new method of enzymic N-acylation of compounds containing amino components.

Polymyxin acylase. An enzyme causing intramolecular N2..LAR..RAR..N6 acyl transfer in-monooctanoyl-L-lysine.