42534-03-2Relevant academic research and scientific papers
Polymyxin Acylase: An Enzyme Causing Intramolecular N2 ->/6 Acyl Transfer in N-Monooctanoyl-L-Lysine
Yasuda, Noriko,Kimura, Yukio,Miyama, Mari,Matsunaga, Hisami
, p. 3245 - 3250 (2007/10/02)
Polymyxin acylase from Pseudomonas sp.M-6-3 can deacylate not only polymyxin antibiotics, but also N-fatty acyl-peptides and N-fatty acyl-amino acids.We found that this enzyme causes intramolecular N2 ->/6 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 acyltransferase 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.
