Multiple modes of active center communication in thiamin diphosphate-dependent enzymes

TitleMultiple modes of active center communication in thiamin diphosphate-dependent enzymes
Publication TypeJournal Article
Year of Publication2005
AuthorsJordan, F, Nemeria NS, Sergienko E
JournalAccounts of Chemical Research
Volume38
Pagination755-763
Date PublishedSep
Type of ArticleReview
ISBN Number0001-4842
Accession Numberhttp://apps.isiknowledge.com/InboundService.do?Func=Frame&product=WOS&action=retrieve&SrcApp=EndNote&Init=Yes&SrcAuth=ResearchSoft&mode=FullRecord&UT=000232094400007
KeywordsACID-BASE GROUPS, ANGSTROM RESOLUTION, BENZOYLFORMATE DECARBOXYLASE, COMPLEX, CRYSTAL-STRUCTURE, DEHYDROGENASE, ESCHERICHIA-COLI, SITES, STRUCTURAL BASIS, SUBSTRATE ACTIVATION, YEAST PYRUVATE-DECARBOXYLASE
Abstract

Detection of interaction between cofactors at the active centers of homodimeric and homotetrameric enzymes is usually elusive by steady-state kinetic approaches and requires protein variants where such interactions are diminished or exaggerated. In this Account, evidence for active-center interactions will be presented for the following thiamin diphosphate-dependent enzymes: yeast pyruvate decarboxylase, benzoylformate decarboxylase, and examples from the 2-oxoacid dehydrogenase multienzyme complex class. The dissymmetry of active sites is especially evident in the X-ray structures of these enzymes with substrate/substrate analogues bound. Perturbations that reveal active center communication include use of chromophoric substrates and substitutions of active center residues on putative pathways.

URLhttp://apps.isiknowledge.com/InboundService.do?Func=Frame&product=WOS&action=retrieve&SrcApp=EndNote&Init=Yes&SrcAuth=ResearchSoft&mode=FullRecord&UT=000232094400007
Alternate JournalAccounts Chem. Res.