| Autor: |
Metz, Renate, Henning, Susanne, Hammes, Walter P. |
| Zdroj: |
Archives of Microbiology; March 1986, Vol. 144 Issue: 2 p181-186, 6p |
| Abstrakt: |
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 Km value of 1×10-4 mol/l. The activity of the ld-carboxypeptidase was inhibited by d-amino acids and the ß-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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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