Specificity of ε-peptidase of Achromobacter pestifer EA

Padayatty, Joseph D. ; Kley, Harold Van (1967) Specificity of ε-peptidase of Achromobacter pestifer EA Archives of Biochemistry and Biophysics, 120 (2). pp. 296-302. ISSN 0003-9861

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000398...

Related URL: http://dx.doi.org/10.1016/0003-9861(67)90242-1


The enzyme ε-acylase/peptidase isolated from Achromobacter pestifer EA was stereospecific for the ε-amide or ε-peptide bonds of L-lysine. The configuration and nature of the amino acid coupled to the ε-amino group of lysine influenced the ε-peptidase activity. The enzymic activity was present if the α-NH2 and α-COOH groups of ε-benzoyl L-lysine and ε- L-phenylalanyl-L-lysine were coordinated with cobalt. The activity was greatly reduced when they were coordinated with copper and was reactivated by the addition of 2-mercaptoethanol or EDTA. The enzymic activity was reduced but not lost if the α-NH2 group was acylated or involved in peptide bond formation. Upon esterification of the α-COOH group with methyl or benzyl groups, the activity was completely lost; there was not much loss of activity when the α-COOH group was combined as a peptide.

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