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Acc Chem Res. 2005 Sep;38(9):755-63.

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

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1
Department of Chemistry, Rutgers, the State University of New Jersey, Newark, New Jersey 07102, USA.

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.

PMID:
16171318
DOI:
10.1021/ar040244e
[Indexed for MEDLINE]
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