PDC6/YGR087C Literature Guide Help

Other names published for PDC6: indolepyruvate decarboxylase 6, YGR087C

PDC6 - Substrates/Ligands/Cofactors (19)

ReferenceOther Genes Addressed
Balakrishnan A, et al.  (2012) Solid-state nuclear magnetic resonance studies delineate the role of the protein in activation of both aromatic rings of thiamin. J Am Chem Soc 134(1):665-72
Romagnoli G, et al.  (2012) Substrate specificity of thiamine pyrophosphate-dependent 2-oxo-acid decarboxylases in Saccharomyces cerevisiae. Appl Environ Microbiol 78(21):7538-48
Kutter S, et al.  (2009) Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation. J Biol Chem 284(18):12136-44
Kong DC, et al.  (2007) [Simulation and analysis of ethanol concentration response to enzyme amount changes in Saccharomyces cerevisiae glycolysis pathway model] Sheng Wu Gong Cheng Xue Bao 23(2):332-6
Kutter S, et al.  (2007) The influence of protein concentration on oligomer structure and catalytic function of two pyruvate decarboxylases. Protein J 26(8):585-91
Joseph E, et al.  (2006) Function of a conserved loop of the beta-domain, not involved in thiamin diphosphate binding, in catalysis and substrate activation in yeast pyruvate decarboxylase. Biochemistry 45(45):13517-27
Jordan F, et al.  (2005) Multiple modes of active center communication in thiamin diphosphate-dependent enzymes. Acc Chem Res 38(9):755-63
van Maris AJ, et al.  (2004) Homofermentative lactate production cannot sustain anaerobic growth of engineered Saccharomyces cerevisiae: possible consequence of energy-dependent lactate export. Appl Environ Microbiol 70(5):2898-905
Sergienko EA and Jordan F  (2002) New model for activation of yeast pyruvate decarboxylase by substrate consistent with the alternating sites mechanism: demonstration of the existence of two active forms of the enzyme. Biochemistry 41(12):3952-67
Sergienko EA and Jordan F  (2001) Catalytic acid-base groups in yeast pyruvate decarboxylase. 2. Insights into the specific roles of D28 and E477 from the rates and stereospecificity of formation of carboligase side products. Biochemistry 40(25):7369-81
Sergienko EA and Jordan F  (2001) Catalytic acid-base groups in yeast pyruvate decarboxylase. 3. A steady-state kinetic model consistent with the behavior of both wild-type and variant enzymes at all relevant pH values. Biochemistry 40(25):7382-403
Neuser F, et al.  (2000) Generation of odorous acyloins by yeast pyruvate decarboxylases and their occurrence in sherry and soy sauce. J Agric Food Chem 48(12):6191-5
Hohmann S and Meacock PA  (1998) Thiamin metabolism and thiamin diphosphate-dependent enzymes in the yeast Saccharomyces cerevisiae: genetic regulation. Biochim Biophys Acta 1385(2):201-19
Dickinson JR, et al.  (1997) A 13C nuclear magnetic resonance investigation of the metabolism of leucine to isoamyl alcohol in Saccharomyces cerevisiae. J Biol Chem 272(43):26871-8
Zeng X, et al.  (1993) Role of cysteines in the activation and inactivation of brewers' yeast pyruvate decarboxylase investigated with a PDC1-PDC6 fusion protein. Biochemistry 32(10):2704-9
Kuo DJ and Jordan F  (1983) Direct spectroscopic observation of a brewer's yeast pyruvate decarboxylase-bound enamine intermediate produced from a suicide substrate. Evidence for nonconcerted decarboxylation. J Biol Chem 258(22):13415-7
Uhlemann H and Schellenberger A  (1976) Glyoxylic acid as an active site marker of yeast pyruvate decarboxylase. FEBS Lett 63(1):37-9
Printz MP and Gounaris AD  (1972) Substrate- and inhibitor-induced conformational changes in enzymes measured by tritium-hydrogen exchange. II. Yeast pyruvate decarboxylase. J Biol Chem 247(22):7109-15
Juni E  (1952) Mechanisms of the formation of acetoin by yeast and mammalian tissue. J Biol Chem 195(2):727-34