Stability of TEM beta-lactamase mutants hydrolyzing third generation cephalosporins.

doi:10.1002/prot.340230108

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Article

Stability of TEM beta-lactamase mutants hydrolyzing third generation cephalosporins.

Proteins - 1 Sept 1995

Raquet X, Vanhove M, Lamotte-Brasseur J, Goussard S, Courvalin P, Frère J M

Abstract excerpt

The stability properties of six natural mutants of the TEM-1 beta-lactamase have been studied. The glutamate to lysine substitution at positions 104 and 240 stabilize the enzyme. Conversely, the G238S mutant's decreased stability might reflect an altered conformation of the active site and thus be related to the modified substrate profile. The relative stability of the R164S and R164H mutants is explained by the...

Topics

Arginine
Cephalosporin Resistance
Cephalosporins
Enzyme Stability
Histidine
Hydrogen-Ion Concentration
Hydrolysis
Models, Chemical
Models, Molecular
Mutation
Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Denaturation

Protein Folding

Serine

Temperature

Thermodynamics

Trypsin

beta-Lactamases

Source

Open in PubMed

Identifiers

PMID: 8539251
DOI: 10.1002/prot.340230108

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