Ontology highlight
ABSTRACT:
SUBMITTER: Huang M
PROVIDER: S-EPMC2522305 | biostudies-literature | 2007 Nov
REPOSITORIES: biostudies-literature
Huang Min M Xie Sheng-Xue SX Ma Ze-Qiang ZQ Huang Qing-Qing QQ Nan Fa-Jun FJ Ye Qi-Zhuang QZ
Journal of medicinal chemistry 20071019 23
Two divalent metal ions are commonly seen in the active-site cavity of methionine aminopeptidase, and at least one of the metal ions is directly involved in catalysis. Although ample structural and functional information is available for dimetalated enzyme, methionine aminopeptidase likely functions as a monometalated enzyme under physiological conditions. Information on structure, as well as catalysis and inhibition, of the monometalated enzyme is lacking. By improving conditions of high-throug ...[more]