Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution
- 1 September 1982
- journal article
- Published by Springer Nature in Nature
- Vol. 299 (5882) , 469-470
- https://doi.org/10.1038/299469a0
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- The exocellular DD‐carboxypeptidase of Streptomyces albus G: A metallo (Zn2+) enzymeFEBS Letters, 1980
- The 4.5 Å resolution structure analysis of the exocellular DD‐carboxypeptidase of Streptomyces albus GFEBS Letters, 1980
- Penicillins and cephalosporins are active site-directed acylating agents: evidence in support of the substrate analogue hypothesisPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1980
- Crystallographic data for the dd-carboxypeptidase-endopeptidase of low penicillin sensitivity excreted by Streptomyces albus GJournal of Molecular Biology, 1979
- Similarities in active center geometries of zinc-containing enzymes, proteases and dehydrogenasesJournal of Molecular Biology, 1978
- Handedness of crossover connections in beta sheets.Proceedings of the National Academy of Sciences, 1976
- Structural patterns in globular proteinsNature, 1976
- Molecular weight, amino acid composition and physicochemical properties of the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R39Biochemical Journal, 1974
- Substrate requirements of the Streptomyces albus G DD carboxypeptidaseBiochemistry, 1970
- The extension of the isomorphous replacement method to include anomalous scattering measurementsActa Crystallographica, 1966