The Molecular Basis of ?-Lactamase Catalysis and Inhibition.
- 1 January 1985
- journal article
- Published by Springer Nature in Pharmaceutical Research
- Vol. 2 (2) , 55-61
- https://doi.org/10.1023/A:1016378325438
Abstract
No abstract availableKeywords
This publication has 62 references indexed in Scilit:
- The reversible deactivation of β-lactamase from Staphylococcus aureus by quinacillin and cephaloridine and its modification by antibodiesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- Crystallographic data for the β-lactamase from Enterobacter cloacae P99Journal of Molecular Biology, 1983
- Inactivation of Bacillus cereus 569/H β-lactamase I by 6-β-(trifluoromethane sulfonyl)amidopenicillanic acid sulfone and its N-methyl derivativeBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Inactivation of β-lactamase I from B. cereus569H with phenylglyoxal, an arginine-selective reagentBiochemical and Biophysical Research Communications, 1982
- Isolation of a covalent intermediate in β-lactamase I catalysisFEBS Letters, 1982
- Synopses from the poster exhibition organized by R. H. Pain 1. New very efficient antibiotics in the field of cephalosporin derivativesPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1980
- Active sites of β-lactamases from Bacillus cereusPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1980
- Penicillinase active sites: Labelling of serine‐44 in β‐lactamase I by 6β‐bromopenicillanic acidFEBS Letters, 1979
- Preliminary crystallographic data for β-lactamase I from Bacillus cereus 569Journal of Molecular Biology, 1978
- The interaction of penicillinase with penicillins I. Effect of substrates and of a competitive inhibitor on native and urea-treated enzymeBiochimica et Biophysica Acta, 1962