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. 1983 Jan 1;209(1):229–233. doi: 10.1042/bj2090229

The inhibition of class C beta-lactamases by boronic acids.

T Beesley, N Gascoyne, V Knott-Hunziker, S Petursson, S G Waley, B Jaurin, T Grundström
PMCID: PMC1154076  PMID: 6405733

Abstract

Aromatic boronic acids are reversible inhibitors of the recently classified class C beta-lactamases. The boronic acids studied include ortho-, meta- and para-methyl-, -hydroxymethyl- and -formyl-phenylboronic acid. The beta-lactamases were chromosomally-encoded enzymes, one from Pseudomonas aeruginosa, and the other specified by the ampC gene of Escherichia coli. The inhibition may be correlated with our finding that these beta-lactamases are serine enzymes, i.e. their function entails the hydroxy group of a serine residue acting as a nucleophile.

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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. Atkins G. L., Nimmo I. A. Current trends in the estimation of Michaelis-Menten parameters. Anal Biochem. 1980 May 1;104(1):1–9. doi: 10.1016/0003-2697(80)90268-7. [DOI] [PubMed] [Google Scholar]
  3. Berks M., Redhead K., Abraham E. P. Isolation and properties of an inducible and a constitutive beta-lactamase from Pseudomonas aeruginosa. J Gen Microbiol. 1982 Jan;128(1):155–159. doi: 10.1099/00221287-128-1-155. [DOI] [PubMed] [Google Scholar]
  4. Bush K., Bonner D. P., Sykes R. B. Izumenolide-a novel beta-lactamase inhibitor produced by Micromonospora. II. Biological properties. J Antibiot (Tokyo) 1980 Nov;33(11):1262–1269. doi: 10.7164/antibiotics.33.1262. [DOI] [PubMed] [Google Scholar]
  5. 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]
  6. 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]
  7. Flett F., Curtis N. A., Richmond M. H. Mutant of Pseudomonas aeruginosa 18S that synthesizes type Id beta-lactamase constitutively. J Bacteriol. 1976 Sep;127(3):1585–1586. doi: 10.1128/jb.127.3.1585-1586.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Kiener P. A., Waley S. G. Reversible inhibitors of penicillinases. Biochem J. 1978 Jan 1;169(1):197–204. doi: 10.1042/bj1690197. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. 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]
  11. 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]
  12. 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]
  13. Knott-Hunziker V., Waley S. G., Orlek B. S., Sammes P. G. Penicillinase active sites: labelling of serine-44 in beta-lactamase I by 6beta-bromopenicillanic acid. FEBS Lett. 1979 Mar 1;99(1):59–61. doi: 10.1016/0014-5793(79)80248-3. [DOI] [PubMed] [Google Scholar]
  14. Linström E. B., Boman H. G., Steele B. B. Resistance of Escherichia coli to penicillins. VI. Purification and characterization of the chromosomally mediated penicillinase present in ampA-containing strains. J Bacteriol. 1970 Jan;101(1):218–231. doi: 10.1128/jb.101.1.218-231.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Matthews D. A., Alden R. A., Birktoft J. J., Freer S. T., Kraut J. X-ray crystallographic study of boronic acid adducts with subtilisin BPN' (Novo). A model for the catalytic transition state. J Biol Chem. 1975 Sep 25;250(18):7120–7126. [PubMed] [Google Scholar]
  16. Nikaido H. Permeability of the outer membrane of bacteria. Angew Chem Int Ed Engl. 1979 May;18(5):337–350. doi: 10.1002/anie.197903373. [DOI] [PubMed] [Google Scholar]
  17. SABATH L. D., ABRAHAM E. P. SYNERGISTIC ACTION OF PENICILLINS AND CEPHALOSPORINS AGAINST PSEUDOMONAS PYOCYANEA. Nature. 1964 Dec 12;204:1066–1069. doi: 10.1038/2041066a0. [DOI] [PubMed] [Google Scholar]
  18. Waley S. G. A quick method for the determination of inhibition constants. Biochem J. 1982 Sep 1;205(3):631–633. doi: 10.1042/bj2050631. [DOI] [PMC free article] [PubMed] [Google Scholar]

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