PDC1/YLR044C Literature Guide Help

Other names published for PDC1: indolepyruvate decarboxylase 1, YLR044C

PDC1 - Protein Physical Properties (55)

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
Morisaka H, et al.  (2012) Two-dimensional protein separation by the HPLC system with a monolithic column. Biosci Biotechnol Biochem 76(3):585-8
Postmus J, et al.  (2012) Isoenzyme expression changes in response to high temperature determine the metabolic regulation of increased glycolytic flux in yeast. FEMS Yeast Res 12(5):571-81
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
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
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
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
Almeida B, et al.  (2009) Yeast protein expression profile during acetic acid-induced apoptosis indicates causal involvement of the TOR pathway. Proteomics 9(3):720-32
Cheng JS, et al.  (2009) Inoculation-density-dependent responses and pathway shifts in Saccharomyces cerevisiae. Proteomics 9(20):4704-13
Cheng JS, et al.  (2009) Proteomic insights into adaptive responses of Saccharomyces cerevisiae to the repeated vacuum fermentation. Appl Microbiol Biotechnol 83(5):909-23
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
Perrot M, et al.  (2009) Yeast proteome map (last update). Proteomics 9(20):4669-73
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
Rossell S, et al.  (2008) Mixed and diverse metabolic and gene-expression regulation of the glycolytic and fermentative pathways in response to a HXK2 deletion in Saccharomyces cerevisiae. FEMS Yeast Res 8(1):155-64
Stevenson BJ, et al.  (2008) Directed evolution of yeast pyruvate decarboxylase 1 for attenuated regulation and increased stability. Biochemistry 47(9):3013-25
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
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
Schowen RL  (2007) Isotopic and other studies on the molecular origins of substrate regulation of some pyruvate decarboxylases: a reconsideration. Isotopes Environ Health Stud 43(1):1-16
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
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
Nemeria N, et al.  (2004) Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1',4'-imino tautomeric form of the coenzyme, unlike the michaelis complex or the free coenzyme. Biochemistry 43(21):6565-75
Fraenkel DG  (2003) The top genes: on the distance from transcript to function in yeast glycolysis. Curr Opin Microbiol 6(2):198-201