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

Frank Jordan, Natalia S. Nemeria, Eduard Sergienko

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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.

Original languageEnglish (US)
Pages (from-to)755-763
Number of pages9
JournalAccounts of Chemical Research
Volume38
Issue number9
DOIs
StatePublished - Sep 1 2005

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All Science Journal Classification (ASJC) codes

  • Chemistry(all)

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