Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1984 Oct 1;223(1):271–274. doi: 10.1042/bj2230271

The active site of the P99 beta-lactamase from Enterobacter cloacae.

B Joris, J Dusart, J M Frere, J van Beeumen, E L Emanuel, S Petursson, J Gagnon, S G Waley
PMCID: PMC1144291  PMID: 6333871

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.

Full text

PDF
274

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ambler R. P. The structure of beta-lactamases. Philos Trans R Soc Lond B Biol Sci. 1980 May 16;289(1036):321–331. doi: 10.1098/rstb.1980.0049. [DOI] [PubMed] [Google Scholar]
  2. Bruton C. J., Hartley B. S. Chemical studies on methionyl-tRNA synthetase from Escherichia coli. J Mol Biol. 1970 Sep 14;52(2):165–178. doi: 10.1016/0022-2836(70)90023-9. [DOI] [PubMed] [Google Scholar]
  3. Campbell D. G., Gagnon J., Reid K. B., Williams A. F. Rat brain Thy-1 glycoprotein. The amino acid sequence, disulphide bonds and an unusual hydrophobic region. Biochem J. 1981 Apr 1;195(1):15–30. doi: 10.1042/bj1950015. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cartwright S. J., Waley S. G. Purification of beta-lactamases by affinity chromatography on phenylboronic acid-agarose. Biochem J. 1984 Jul 15;221(2):505–512. doi: 10.1042/bj2210505. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cartwright S. J., Waley S. G. beta-Lactamase inhibitors. Med Res Rev. 1983 Oct-Dec;3(4):341–382. doi: 10.1002/med.2610030402. [DOI] [PubMed] [Google Scholar]
  6. Charlier P., Dideberg O., Frère J. M., Moews P. C., Knox J. R. Crystallographic data for the beta-lactamase from Enterobacter cloacae P99. J Mol Biol. 1983 Dec 5;171(2):237–238. doi: 10.1016/s0022-2836(83)80358-1. [DOI] [PubMed] [Google Scholar]
  7. Cohen S. A., Pratt R. F. Inactivation of Bacillus cereus beta-lactamase I by 6 beta-bromopencillanic acid: mechanism. Biochemistry. 1980 Aug 19;19(17):3996–4003. doi: 10.1021/bi00558a017. [DOI] [PubMed] [Google Scholar]
  8. Fisher J., Belasco J. G., Khosla S., Knowles J. R. beta-Lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitin. Biochemistry. 1980 Jun 24;19(13):2895–2901. doi: 10.1021/bi00554a012. [DOI] [PubMed] [Google Scholar]
  9. Fisher J., Charnas R. L., Bradley S. M., Knowles J. R. Inactivation of the RTEM beta-lactamase from Escherichia coli. Interaction of penam sulfones with enzyme. Biochemistry. 1981 May 12;20(10):2726–2731. doi: 10.1021/bi00513a004. [DOI] [PubMed] [Google Scholar]
  10. Hewick R. M., Hunkapiller M. W., Hood L. E., Dreyer W. J. A gas-liquid solid phase peptide and protein sequenator. J Biol Chem. 1981 Aug 10;256(15):7990–7997. [PubMed] [Google Scholar]
  11. Jaurin B., Grundström T. ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4897–4901. doi: 10.1073/pnas.78.8.4897. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Knott-Hunziker V., Orlek B. S., Sammes P. G., Waley S. G. 6 beta-Bromopenicillanic acid inactivates beta-lactamase I. Biochem J. 1979 Jan 1;177(1):365–367. doi: 10.1042/bj1770365. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Knott-Hunziker V., Orlek B. S., Sammes P. G., Waley S. G. Kinetics of inactivation of beta-lactamase I by 6 beta-bromopenicillanic acid. Biochem J. 1980 Jun 1;187(3):797–802. doi: 10.1042/bj1870797. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Knott-Hunziker V., Petursson S., Jayatilake G. S., Waley S. G., Jaurin B., Grundström T. Active sites of beta-lactamases. The chromosomal beta-lactamases of Pseudomonas aeruginosa and Escherichia coli. Biochem J. 1982 Mar 1;201(3):621–627. doi: 10.1042/bj2010621. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Knott-Hunziker V., Petursson S., Waley S. G., Jaurin B., Grundström T. The acyl-enzyme mechanism of beta-lactamase action. The evidence for class C Beta-lactamases. Biochem J. 1982 Nov 1;207(2):315–322. doi: 10.1042/bj2070315. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Offord R. E. The use of logarithmic plots of electrophoretic mobilities of peptides. Methods Enzymol. 1977;47:51–69. doi: 10.1016/0076-6879(77)47008-3. [DOI] [PubMed] [Google Scholar]
  17. Ross G. W. Beta-lactamase (Enterobacter species). Methods Enzymol. 1975;43:678–687. doi: 10.1016/0076-6879(75)43133-0. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES