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000094208 1001_ $$aKutter, S.
000094208 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000094208 245__ $$aCovalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme Activation
000094208 260__ $$aBethesda, Md.$$bSoc.$$c2009
000094208 300__ $$a12136-12144
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000094208 440_0 $$0PERI:(DE-600)1474604-9$$aJ. Biol. Chem.$$v284$$x0021-9258
000094208 500__ $$3Converted on 2013-05-30 14:57
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000094208 520__ $$aThe mechanism by which the enzyme pyruvate decarboxylase from two yeast species is activated allosterically has been elucidated. A total of seven three-dimensional structures of the enzyme, of enzyme variants, or of enzyme complexes from two yeast species, three of them reported here for the first time, provide detailed atomic resolution snapshots along the activation coordinate. The prime event is the covalent binding of the substrate pyruvate to the side chain of cysteine 221, thus forming a thiohemiketal. This reaction causes the shift of a neighboring amino acid, which eventually leads to the rigidification of two otherwise flexible loops, one of which provides two histidine residues necessary to complete the enzymatically competent active site architecture. The structural data are complemented and supported by kinetic investigations and binding studies, providing a consistent picture of the structural changes occurring upon enzyme activation.
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000094208 650_2 $$2MeSH$$aAllosteric Regulation: physiology
000094208 650_2 $$2MeSH$$aEnzyme Activation: physiology
000094208 650_2 $$2MeSH$$aFungal Proteins: chemistry
000094208 650_2 $$2MeSH$$aKinetics
000094208 650_2 $$2MeSH$$aKluyveromyces: enzymology
000094208 650_2 $$2MeSH$$aProtein Structure, Tertiary: physiology
000094208 650_2 $$2MeSH$$aPyruvate Decarboxylase: chemistry
000094208 650_2 $$2MeSH$$aPyruvic Acid: chemistry
000094208 650_7 $$00$$2NLM Chemicals$$aFungal Proteins
000094208 650_7 $$0127-17-3$$2NLM Chemicals$$aPyruvic Acid
000094208 650_7 $$0EC 4.1.1.1$$2NLM Chemicals$$aPyruvate Decarboxylase
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000094208 7001_ $$aWeiss, M. S.
000094208 7001_ $$aWille, G.
000094208 7001_ $$aGolbik, R.
000094208 7001_ $$aSpinka, M.
000094208 7001_ $$aKönig, S.
000094208 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M806228200$$gVol. 284, p. 12136-12144$$p12136-12144$$q284<12136-12144$$tThe @journal of biological chemistry$$v284$$x0021-9258$$y2009
000094208 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2673282
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