Interaction of the pBR 322-coded RTEM α-lactamase with substrates. Evidence for specific conformational transitions.
- 31 January 1982
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 201 (2), 425-427
- https://doi.org/10.1042/bj2010425
Abstract
The rate of inactivation of RTEM-1 beta-lactamase by Pronase is accelerated by class A (‘resistant’) penicillins. Other substrates (class S penicillin and cephalosporins) protect against the inactivation. Cefoxitin, a semi-synthetic cephamycin, induces a more extensive, hysteretic response. In its presence the enzyme is inactivated by trypsin as well as by Pronase.This publication has 18 references indexed in Scilit:
- Catalytic and conformational properties of cross-linked derivatives of penicillinaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1979
- Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322.Proceedings of the National Academy of Sciences, 1978
- Partial amino acid sequence of penicillinase coded by Escherichia coli plasmid R6K.Proceedings of the National Academy of Sciences, 1978
- Kinetic studies on the inactivation of Escherichia coli RTEM β-lactamase by clavulanic acidBiochemistry, 1978
- Acquisition of substrate-specific parameters during the catalytic reaction of penicillinase.Proceedings of the National Academy of Sciences, 1976
- Conformational Adaptability in EnzymesPublished by Wiley ,1973
- Preparation of gram quantities of a purified R-factor-mediated penicillinase from Escherichia coli strain W3310Biochemical Journal, 1972
- Purification and properties of the γ-type β-lactamase of Bacillus cereusArchives of Biochemistry and Biophysics, 1967
- Penicillinase Synthesis Controlled By Infectious R Factors In EnterobacteriaceaeNature, 1965
- The interaction of penicillinase with penicillins IV. Structural aspects of catalytic and non-catalytic interactionsBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965