Probing the determinants of protein stability: comparison of class A beta-lactamases

Five class A beta-lactamases produced by various mesophilic bacterial species have been compared. Although closely related in primary and overall structures, these enzymes exhibit very different stabilities. In order to investigate the factors responsible for these differences, several features dedu...

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Bibliographic Details
Published in:Biochemical journal 1995-06, Vol.308 ( Pt 3) (3), p.859-864
Main Authors: Vanhove, M, Houba, S, b1motte-Brasseur, J, Frère, J M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - analysis
Bacteria - enzymology
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
beta-Lactamases - chemistry
beta-Lactamases - classification
beta-Lactamases - metabolism
Crystallography
Enzyme Stability - genetics
Enzyme Stability - physiology
Fungal Proteins - chemistry
Fungal Proteins - metabolism
Fungi - enzymology
Hydrogen Bonding
Molecular Sequence Data
Protein Folding
Protein Structure, Tertiary
Sequence Alignment
Temperature
Thermodynamics
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Summary:Five class A beta-lactamases produced by various mesophilic bacterial species have been compared. Although closely related in primary and overall structures, these enzymes exhibit very different stabilities. In order to investigate the factors responsible for these differences, several features deduced from the amino acid composition and three-dimensional structures were studied for the five proteins. This analysis revealed that higher stability appeared to correlate with increased numbers of intramolecular hydrogen bonds and of salt bridges. By contrast, the global hydrophobicity of the protein seemed to play a relatively minor role. A strongly unfavourable balance between charged residues and the presence of a cis-peptide bond preceding a non-proline residue might also contribute to the particularly low stability of two of the enzymes.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj3080859