QM/MM studies of monozinc β-lactamase CphA suggest that the crystal structure of an enzyme-intermediate complex represents a minor pathway.
QM/MM studies of the hydrolysis of a β-lactam antibiotic molecule (biapenem) catalyzed by a monozinc β-lactamase (CphA) have revealed the complete reaction mechanism and shown that an experimentally determined enzyme-intermediate complex is a stable intermediate or product in a minor pathway.
MOE Key Laboratory of Green Chemistry and Technology, College of Chemistry, Sichuan University, Chengdu, Sichuan 610064, P. R. China.
Shanshan
S
Wu
Dingguo
D
Xu
Hua
H
Guo
D001426:Bacterial Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D011789:Quantum Theory; D013379:Substrate Specificity; D015032:Zinc / Q000737:chemistry; D001618:beta-Lactamases / Q000737:chemistry*
D001426:Bacterial Proteins; D001618:beta-Lactamases; C082063:cphA protein, Aeromonas hydrophila; D015032:Zinc