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PMID: 6049371 Published · ppublish English Journal Article

Substrate-specific inactivation of staphylococcal penicillinase.

The Biochemical journal ·Vol. 103 ·No. 3 ·1967-06-00 ·Pages 641-6

Dyke KG

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.

MeSH Terms
Chemical Phenomena Chemistry Cloxacillin/metabolism Enzyme Induction Hydrogen-Ion Concentration Immune Sera Kinetics Methicillin/metabolism Penicillinase/metabolism Penicillins/metabolism Quinoxalines/metabolism Staphylococcus/enzymology beta-Lactamase Inhibitors
Chemicals
Immune Sera Penicillins Quinoxalines beta-Lactamase Inhibitors Penicillinase Cloxacillin Methicillin
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Dyke K G
References (14)
14 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1967-06-00
Pages
641-6
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1270462
Subset
IM
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