Jump to Main Content
- van der Kamp, Marc W., et al. Show all 8 Authors
- Journal of the American Chemical Society 2018 v.140 no.46 pp. 15889-15903
- Saccharomyces cerevisiae; active sites; catalytic activity; crystal structure; molecular dynamics; sampling; simulation models; triose-phosphate isomerase
- ... Conformational changes are crucial for the catalytic action of many enzymes. A prototypical and well-studied example is loop opening and closure in triosephosphate isomerase (TIM), which is thought to determine the rate of catalytic turnover in many circumstances. Specifically, TIM loop 6 “grips” the phosphodianion of the substrate and, together with a change in loop 7, sets up the TIM active site ...
- van der Kamp, Marc W., et al. Show all 6 Authors
- Journal of the American Chemical Society 2012 v.134 no.44 pp. 18275-18285
- Gram-negative bacteria; Serratia; active sites; beta-lactamase; crystal structure; crystallography; drugs; hydrolysis; meropenem; molecular dynamics; mutants
- ... Carbapenems are the most potent β-lactam antibiotics and key drugs for treating infections by Gram-negative bacteria. In such organisms, β-lactam resistance arises principally from β-lactamase production. Although carbapenems escape the activity of most β-lactamases, due in the class A enzymes to slow deacylation of the covalent acylenzyme intermediate, carbapenem-hydrolyzing class A β-lactamases ...