Abstract:
: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 sulfate-polyacrylamide 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 Km value of 1 X 10(-4) mol/l. The activity of the LD-carboxypeptidase was inhibited by D-amino acids and the beta-lactam antibiotic nocardicin A. Ki values of 0.3 and 43 mmol/l were determined for nocardicin A and D-homoserine, respectively. The properties of the purified enzyme correspond to activity I in ether treated cells.
journal_name
Arch Microbioljournal_title
Archives of microbiologyauthors
Metz R,Henning S,Hammes WPdoi
10.1007/BF00414732subject
Has Abstractpub_date
1986-03-01 00:00:00pages
181-6issue
2eissn
0302-8933issn
1432-072Xjournal_volume
144pub_type
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