Ontology highlight
ABSTRACT:
SUBMITTER: Fernandez D
PROVIDER: S-EPMC3144702 | biostudies-literature | 2011
REPOSITORIES: biostudies-literature
Fernández Daniel D Boix Ester E Pallarès Irantzu I Avilés Francesc X FX Vendrell Josep J
Enzyme research 20110725
A high-resolution carboxypeptidase-Zn(2+)-citrate complex was studied by X-ray diffraction and enzyme kinetics for the first time. The citrate molecule acts as a competitive inhibitor of this benchmark zinc-dependent peptidase, chelating the catalytic zinc ion in the active site of the enzyme and inducing a conformational change such that carboxypeptidase adopts the conformation expected to occur by substrate binding. Citrate adopts an extended conformation with half of the molecule facing the z ...[more]