A bifunctional monocyclic beta-lactam cross-links across the active site of beta-lactamase.
(1995)
Journal - Biochemical and biophysical research communications (UNITED STATES )
Abstract :
A 4-alkoxy-2-azetidinone behaves as a bifunctional active site-directed inhibitor of the class A beta-lactamase from Bacillus cereus 569/H. It cross-links SER 70 and LYS 234 as it binds in a approximately 1:1 ratio. The cross-linked enzyme is irreversibly inhibited while the secondary structure is partially stabilized under conditions when the native enzyme is otherwise converted to a form with no detectable secondary structure by circular dichroism.
| ISSN : | 0006-291X |
|---|
| Mesh Heading : | Acetamides Amino Acid Sequence Azetidines Bacillus cereus Binding Sites Circular Dichroism Cross-Linking Reagents Lysine Mass Spectrometry Models, Molecular Molecular Sequence Data Molecular Structure Peptide Fragments Peptide Mapping Serine beta-Lactamases chemical synthesis chemistry chemical synthesis chemistry enzymology chemistry |
|---|
| Mesh Heading Relevant : | Protein Structure, Secondary metabolism metabolism antagonists & inhibitors chemistry |
|---|