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 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 1×10-4 mol/l. The activity of the ld-carboxypeptidase was inhibited by d-amino acids and the β-lactam antibiotic nocardicin A. K i 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.
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Abbreviations
- MurNAc:
-
N-acetylmuramyl
- GlcNAc:
-
N-acetylglucosamine; tetrapeptide
- AGD(L)A:
-
Ala DGlu-meso-Dap(Lys)
- DAla:
-
pentapeptide
- AGD(L)AA:
-
Ala-DGlu-meso-Dap(Lys)-DAla-DAla
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Metz, R., Henning, S. & Hammes, W.P. ld-Carboxypeptidase activity in Escherichia coli . Arch. Microbiol. 144, 181–186 (1986). https://doi.org/10.1007/BF00414732
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DOI: https://doi.org/10.1007/BF00414732