Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1967 Jun;103(3):641–646. doi: 10.1042/bj1030641

Substrate-specific inactivation of staphylococcal penicillinase

K G H Dyke 1
PMCID: PMC1270462  PMID: 6049371

Abstract

1. The rate of hydrolysis of methicillin, cloxacillin and quinacillin by staphylococcal extracellular penicillinase decreases progressively with time. 2. The inactivation is prevented but not reversed by benzylpenicillin. 3. The rate of inactivation produced by quinacillin is minimal when the rate of hydrolysis is at a maximum. 4. Under certain conditions, partially inactivated enzyme can be reactivated. 5. Combination of the enzyme with antiserum, while permitting hydrolysis, prevents inactivation. 6. No evidence for a stable enzyme–substrate complex has been found.

Full text

PDF
641

Selected References

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

  1. BATCHELOR F. R., CAMERON-WOOD J., CHAIN E. B., ROLINSON G. N. STUDIES ON PENICILLINASE PRODUCED BY A STRAIN OF STAPHYLOCOCCUS AUREUS. Proc R Soc Lond B Biol Sci. 1963 Oct 22;158:311–328. doi: 10.1098/rspb.1963.0050. [DOI] [PubMed] [Google Scholar]
  2. CITRI N., GARBER N., KALKSTEIN A. THE INTERACTION OF PENICILLINASE WITH PENICILLINS. 3. COMPARISON OF EXOPENICILLINASE PREPARATIONS OF VARIOUS ORIGINS. Biochim Biophys Acta. 1964 Dec 23;92:572–581. doi: 10.1016/0926-6569(64)90017-3. [DOI] [PubMed] [Google Scholar]
  3. CROMPTON B., JAGO M., CRAWFORD K., NEWTON G. G., ABRAHAM E. P. Behaviour of some derivatives of 7-aminocephalosporanic acid and 6-aminopenicillanic acidas substrates, inhibitors and inducers of penicillinases. Biochem J. 1962 Apr;83:52–63. doi: 10.1042/bj0830052. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Citri N., Zyk N. The interaction of penicillinase with penicillins. IV. Structural aspects of catalytic and non-catalytic interactions. Biochim Biophys Acta. 1965 Jun 22;99(3):427–441. doi: 10.1016/s0926-6593(65)80197-7. [DOI] [PubMed] [Google Scholar]
  5. GOUREVITCH A., PURSIANO T. A., LEIN J. Inactivation of staphylococcal penicillinase by reaction with resistant penicillins. Nature. 1962 Aug 4;195:496–497. doi: 10.1038/195496a0. [DOI] [PubMed] [Google Scholar]
  6. NOVICK R. P. ANALYSIS BY TRANSDUCTION OF MUTATIONS AFFECTING PENICILLINASE FORMATION IN STAPHYLOCOCCUS AUREUS. J Gen Microbiol. 1963 Oct;33:121–136. doi: 10.1099/00221287-33-1-121. [DOI] [PubMed] [Google Scholar]
  7. NOVICK R. P. Micro-iodometric assay for penicillinase. Biochem J. 1962 May;83:236–240. doi: 10.1042/bj0830236. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. NOVICK R. P. Staphylococcal penicillinase and the new penicillins. Biochem J. 1962 May;83:229–235. doi: 10.1042/bj0830229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. PERRET C. J. Iodometric assay of penicillinase. Nature. 1954 Nov 27;174(4439):1012–1013. doi: 10.1038/1741012a0. [DOI] [PubMed] [Google Scholar]
  10. POLLOCK M. R. Penicillinase adaptation in B. cereus; adaptive enzyme formation in the absence of free substrate. Br J Exp Pathol. 1950 Dec;31(6):739–753. [PMC free article] [PubMed] [Google Scholar]
  11. POLLOCK M. R. STIMULATING AND INHIBITING ANTIBODIES FOR BACTERIAL PENICILLINASE. Immunology. 1964 Nov;7:707–723. [PMC free article] [PubMed] [Google Scholar]
  12. RICHARDS H. C., HOUSLEY J. R., SPOONER D. F. QUINACILLIN: A NEW PENICILLIN WITH UNUSUAL PROPERTIES. Nature. 1963 Jul 27;199:354–356. doi: 10.1038/199354a0. [DOI] [PubMed] [Google Scholar]
  13. RICHMOND M. H. PURIFICATION AND PROPERTIES OF THE EXOPENICILLINASE FROM STAPHYLOCOCCUS AUREUS. Biochem J. 1963 Sep;88:452–459. doi: 10.1042/bj0880452. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. ROGERS H. J. Variant populations within a hyaluronidase-producing culture of Staphylococcus aureus. J Pathol Bacteriol. 1953 Oct;66(2):545–551. doi: 10.1002/path.1700660226. [DOI] [PubMed] [Google Scholar]

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

RESOURCES