Article
Determinants of binding affinity and specificity for the interaction of TEM-1 and SME-1 beta-lactamase with beta-lactamase inhibitory protein.
The Journal of biological chemistry - 14 Nov 2003
Zhang Zhen, Palzkill Timothy
Abstract excerpt
The hydrolysis of beta-lactam antibiotics by class A beta-lactamases is a common cause of bacterial resistance to these agents. The beta-lactamase inhibitory protein (BLIP) is able to bind and inhibit several class A beta-lactamases, including TEM-1 beta-lactamase and SME-1 beta-lactamase. Although the TEM-1 and SME-1 enzymes share 33% amino acid sequence identity and a similar fold, they differ substantially in...
Topics
- Alanine
- Bacterial Proteins
- Binding Sites
- Dose-Response Relationship, Drug
- Electrophoresis, Polyacrylamide Gel
- Epitopes
- Escherichia coli
- Glutamic Acid
- Hydrolysis
- Kinetics
- Lysine
- Models, Molecular
- Mutagenesis
- Mutation
- Plasmids
- Polymerase Chain Reaction
- Protein Binding
- Protein Conformation