PDC5/YLR134W Literature Guide Help

Other names published for PDC5: indolepyruvate decarboxylase 5, YLR134W

PDC5 - Protein Physical Properties (24)

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
Swainston N, et al.  (2011) A QconCAT informatics pipeline for the analysis, visualization and sharing of absolute quantitative proteomics data. Proteomics 11(2):329-33
van Eunen K, et al.  (2010) Measuring enzyme activities under standardized in vivo-like conditions for systems biology. FEBS J 277(3):749-60
van Eunen K, et al.  (2010) Time-dependent regulation of yeast glycolysis upon nitrogen starvation depends on cell history. IET Syst Biol 4(2):157
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
van Eunen K, et al.  (2009) Time-dependent regulation analysis dissects shifts between metabolic and gene-expression regulation during nitrogen starvation in baker's yeast. FEBS J 276(19):5521-36
Mirzaei H and Regnier F  (2008) Protein:protein aggregation induced by protein oxidation. J Chromatogr B Analyt Technol Biomed Life Sci 873(1):8-14
Tylicki A, et al.  (2008) Comparative study of the activity and kinetic properties of malate dehydrogenase and pyruvate decarboxylase from Candida albicans, Malassezia pachydermatis, and Saccharomyces cerevisiae. Can J Microbiol 54(9):734-41
van den Brink J, et al.  (2008) Dynamics of glycolytic regulation during adaptation of Saccharomyces cerevisiae to fermentative metabolism. Appl Environ Microbiol 74(18):5710-23
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
Rossell S, et al.  (2006) Unraveling the complexity of flux regulation: a new method demonstrated for nutrient starvation in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 103(7):2166-71
Jordan F, et al.  (2005) Multiple modes of active center communication in thiamin diphosphate-dependent enzymes. Acc Chem Res 38(9):755-63
Fraenkel DG  (2003) The top genes: on the distance from transcript to function in yeast glycolysis. Curr Opin Microbiol 6(2):198-201
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  (2002) Yeast pyruvate decarboxylase tetramers can dissociate into dimers along two interfaces. Hybrids of low-activity D28A (or D28N) and E477Q variants, with substitution of adjacent active center acidic groups from different subunits, display restored activity. Biochemistry 41(19):6164-9
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
Hohmann S and Cederberg H  (1990) Autoregulation may control the expression of yeast pyruvate decarboxylase structural genes PDC1 and PDC5. Eur J Biochem 188(3):615-21
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
Banuelos M and Gancedo C  (1978) In situ study of the glycolytic pathway in Saccharomyces cerevisiae. Arch Microbiol 117(2):197-201
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
Jones RC and Hough JS  (1970) The effect of temperature on the metabolism of baker's yeast growing on continuous culture. J Gen Microbiol 60(1):107-16
Juni E  (1952) Mechanisms of the formation of acetoin by yeast and mammalian tissue. J Biol Chem 195(2):727-34