The active site of the P99 β-lactamase from Enterobacter cloacae
- 1 October 1984
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 223 (1), 271-274
- https://doi.org/10.1042/bj2230271
Abstract
Labelling the beta-lactamase of Enterobacter cloacae P99 with a poor substrate or a mechanism-based inactivator points to an active-site serine residue in a sequence closely resembling that of the ampC beta-lactamase. These results establish the P99 enzyme as a class-C beta-lactamase, and the concurrence of the two approaches helps to confirm the reliability of determining active-site sequences with the aid of mechanism-based inactivators.This publication has 17 references indexed in Scilit:
- A gas-liquid solid phase peptide and protein sequenator.Journal of Biological Chemistry, 1981
- ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type.Proceedings of the National Academy of Sciences, 1981
- Inactivation of the RTEM .beta.-lactamase from Escherichia coli. Interaction of penam sulfones with the enzymeBiochemistry, 1981
- Rat brain Thy-1 glycoprotein. The amino acid sequence, disulphide bonds and an unusual hydrophobic regionBiochemical Journal, 1981
- Inactivation of Bacillus cereus .beta.-lactamase I by 6.beta.-bromopenicillanic acid: mechanismBiochemistry, 1980
- .beta.-Lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitinBiochemistry, 1980
- 6 β-Bromopenicillanic acid inactivates β-lactamase IBiochemical Journal, 1979
- [6] The use of logarithmic plots of electrophoretic mobilities of peptidesMethods in Enzymology, 1977
- [53e] β-Lactamase (Enterobacter species)Methods in Enzymology, 1975
- Chemical studies on methionyl-tRNA synthetase from Escherichia coliJournal of Molecular Biology, 1970