The 4.5 Å resolution structure analysis of the exocellular DD‐carboxypeptidase of Streptomyces albus G
- 11 August 1980
- journal article
- Published by Wiley in FEBS Letters
- Vol. 117 (1-2) , 212-214
- https://doi.org/10.1016/0014-5793(80)80947-1
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
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- Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.Proceedings of the National Academy of Sciences, 1979
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- Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.Proceedings of the National Academy of Sciences, 1977
- Occurrence of a serine residue in the penicillin‐binding site of the exocellular DD‐carboxy‐peptidase‐transpeptidase from Streptomyces R61FEBS Letters, 1976
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- A semi-empirical method of absorption correctionActa Crystallographica Section A, 1968