PDC1/YLR044C Literature Guide Help

Other names published for PDC1: indolepyruvate decarboxylase 1, YLR044C

PDC1 - Substrates/Ligands/Cofactors (48)

Results: 1 - 30 of 48 records
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ReferenceOther Genes Addressed
Balakrishnan A, et al.  (2012) Bifunctionality of the thiamin diphosphate cofactor: assignment of tautomeric/ionization states of the 4'-aminopyrimidine ring when various intermediates occupy the active sites during the catalysis of yeast pyruvate decarboxylase. J Am Chem Soc 134(8):3873-85
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
Kondo T, et al.  (2012) Genetic engineering to enhance the Ehrlich pathway and alter carbon flux for increased isobutanol production from glucose by Saccharomyces cerevisiae. J Biotechnol 159(1-2):32-7
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
Stevenson BJ, et al.  (2012) Fermentative glycolysis with purified Escherichia coli enzymes for in vitro ATP production and evaluating an engineered enzyme. J Biotechnol 157(1):113-23
K Suresh K, et al.  (2011) Comparative and chemical proteomic approaches reveal gatifloxacin deregulates enzymes involved in glucose metabolism. J Toxicol Sci 36(6):787-96
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
Stevenson BJ, et al.  (2008) Directed evolution of yeast pyruvate decarboxylase 1 for attenuated regulation and increased stability. Biochemistry 47(9):3013-25
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
Nemeria N, et al.  (2007) The 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes. Proc Natl Acad Sci U S A 104(1):78-82
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
Wang J, et al.  (2005) Theoretical Study toward Understanding the Catalytic Mechanism of Pyruvate Decarboxylase. J Phys Chem B Condens Matter Mater Surf Interfaces Biophys 109(39):18664-18672
Casas JS, et al.  (2004) The reaction of dimethyltin(IV) dichloride with thiamine diphosphate (H2TDP): synthesis and structure of [SnMe2(HTDP)(H2O)]Cl.H2O, and possibility of a hitherto unsuspected role of the metal cofactor in the mechanism of vitamin-B1-dependent enzymes. Inorg Chem 43(6):1957-63
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
Jordan F, et al.  (2002) Spectroscopic evidence for participation of the 1',4'-imino tautomer of thiamin diphosphate in catalysis by yeast pyruvate decarboxylase. Bioorg Chem 30(3):188-98
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
Liu M, et al.  (2001) Catalytic acid-base groups in yeast pyruvate decarboxylase. 1. Site-directed mutagenesis and steady-state kinetic studies on the enzyme with the D28A, H114F, H115F, and E477Q substitutions. Biochemistry 40(25):7355-68
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
Wang J, et al.  (2001) Consequences of a modified putative substrate-activation site on catalysis by yeast pyruvate decarboxylase. Biochemistry 40(6):1755-63
Cabiscol E, et al.  (2000) Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J Biol Chem 275(35):27393-8
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
Peter Smits H, et al.  (2000) Simultaneous overexpression of enzymes of the lower part of glycolysis can enhance the fermentative capacity of Saccharomyces cerevisiae. Yeast 16(14):1325-34
Teusink B, et al.  (2000) Can yeast glycolysis be understood in terms of in vitro kinetics of the constituent enzymes? Testing biochemistry. Eur J Biochem 267(17):5313-29
Eberhardt I, et al.  (1999) Autoregulation of yeast pyruvate decarboxylase gene expression requires the enzyme but not its catalytic activity. Eur J Biochem 262(1):191-201
Li H and Jordan F  (1999) Effects of substitution of tryptophan 412 in the substrate activation pathway of yeast pyruvate decarboxylase. Biochemistry 38(31):10004-12
Li H, et al.  (1999) Role of glutamate 91 in information transfer during substrate activation of yeast pyruvate decarboxylase. Biochemistry 38(31):9992-10003
Dickinson JR, et al.  (1998) An investigation of the metabolism of valine to isobutyl alcohol in Saccharomyces cerevisiae. J Biol Chem 273(40):25751-6
Results: 1 - 30 of 48 records
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