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PMID: 3931629 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The production and molecular properties of the zinc beta-lactamase of Pseudomonas maltophilia IID 1275.

The Biochemical journal ·Vol. 229 ·No. 3 ·1985-08-01 ·Pages 791-7

Bicknell R, Emanuel EL, Gagnon J, Waley SG

Abstract

The production and purification of a tetrameric zinc beta-lactamase from Pseudomonas maltophilia IID 1275 were greatly improved. Three charge variants were isolated by chromatofocusing. The subunits each contain two atomic proportions of zinc and (in two of the variants) one residue of cysteine. The thiol group is not required for activity, nor does it appear to bind to the metal. Replacement of zinc by cobalt, cadmium or nickel takes place at a measurable rate, and gives enzymes that are less active than the zinc enzyme. The properties of this enzyme differ from those of the other known zinc beta-lactamase, beta-lactamase II from Bacillus cereus. The amino acid sequence of the N-terminal 32 residues was determined; there is no similarity to the N-terminal sequences of other beta-lactamases.

MeSH Terms
Amino Acids/analysis Cations, Divalent/pharmacology Cephalosporinase/metabolism Chromatography, Gel Edetic Acid/pharmacology Kinetics Pseudomonas/enzymology Spectrophotometry Zinc/metabolism beta-Lactamase Inhibitors beta-Lactamases/isolation & purification,metabolism
Chemicals
Amino Acids Cations, Divalent beta-Lactamase Inhibitors Edetic Acid Cephalosporinase beta-Lactamases Zinc
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Bicknell R
Emanuel E L
Gagnon J
Waley S G
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2290791
Published
1985-08-01
Pages
791-7
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1145126
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2290791 PMC Full Text View journal details
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