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ld-Carboxypeptidase activity inEscherichia coli

โœ Scribed by Renate Metz; Susanne Henning; Walter P. Hammes

Publisher
Springer
Year
1986
Tongue
English
Weight
559 KB
Volume
144
Category
Article
ISSN
0302-8933

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โœฆ Synopsis

A LD-carboxypeptidase from Escherichia coli K 12 was isolated by Tris-EDTA treatment and purified to electrophoretic homogeneity by DEAE-cellulose chromatography. The enzyme has a molecular weight of approximately 12,000 as determined by sodium dodecyl sulfatepolyacrylamide electrophoresis and by Sephadex G-100 gel filtration. The studies of the substrate specificity of the enzyme revealed that UDP-MurNAc-tetrapeptide is a superior substrate, with a K m value of 1 x 1 0 -4 tool/1. The activity of the LD-carboxypeptidase was inhibited by D-amino acids and the fi-lactam antibiotic nocardicin A. Ki values of 0.3 and 43 retool/1 were determined for nocardicin A and D-homoserine, respectively. The properties of the purified enzyme correspond to activity I in ether treated cells.

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