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PMID: 2302162 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

The diversity of the catalytic properties of class A beta-lactamases.

The Biochemical journal ·Vol. 265 ·No. 1 ·1990-01-01 ·Pages 131-46

Matagne A, Misselyn-Bauduin AM, Joris B, Erpicum T, Granier B, Frère JM

Abstract

The catalytic properties of four class A beta-lactamases were studied with 24 different substrates. They exhibit a wide range of variation. Similarly, the amino acid sequences are also quite different. However, no relationships were found between the sequence similarities and the substrate profiles. Lags and bursts were observed with various compounds containing a large sterically hindered side chain. As a group, the enzymes could be distinguished from the class C beta-lactamases on the basis of the kappa cat. values for several substrates, particularly oxacillin, cloxacillin and carbenicillin. Surprisingly, that distinction was impossible with the kappa cat./Km values, which represent the rates of acylation of the active-site serine residue by the beta-lactam. For several cephalosporin substrates (e.g. cefuroxime and cefotaxime) class A enzymes consistently exhibited higher kappa cat. values than class C enzymes, thus belying the usual distinction between 'penicillinases' and 'cephalosporinases'. The problem of the repartition of class A beta-lactamases into sub-classes is discussed.

MeSH Terms
Amino Acid Sequence Bacillus/enzymology Catalysis Chemical Phenomena Chemistry Enterobacter/enzymology Enzyme Stability Kinetics Molecular Sequence Data Nocardiaceae/enzymology Sequence Homology, Nucleic Acid Streptomyces/enzymology Substrate Specificity beta-Lactamase Inhibitors beta-Lactamases/metabolism
Chemicals
beta-Lactamase Inhibitors beta-Lactamases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Matagne A
Université de Liège, Institute de Chimie, Belgium.
Misselyn-Bauduin A M
Joris B
Erpicum T
Granier B
Frère J M
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2650131
Published
1990-01-01
Pages
131-46
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1136623
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2650131 PMC Full Text View journal details
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