PDC1/YLR044C Literature Guide Help

Other names published for PDC1: indolepyruvate decarboxylase 1, YLR044C

PDC1 - Protein Sequence Features (28)

ReferenceOther Genes Addressed
Foyn H, et al.  (2013) Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo. Mol Cell Proteomics 12(1):42-54
Lesur A, et al.  (2012) Peptides quantification by liquid chromatography with matrix-assisted laser desorption/ionization and selected reaction monitoring detection. J Proteome Res 11(10):4972-82
Brandes N, et al.  (2011) Using quantitative redox proteomics to dissect the yeast redoxome. J Biol Chem 286(48):41893-903
Carroll KM, et al.  (2011) Absolute quantification of the glycolytic pathway in yeast: deployment of a complete QconCAT approach. Mol Cell Proteomics 10(12):M111.007633
Kim JH, et al.  (2010) Dynamics of protein damage in yeast frataxin mutant exposed to oxidative stress. OMICS 14(6):689-99
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
Shrestha A, et al.  (2010) Modeling of pyruvate decarboxylases from ethanol producing bacteria. Bioinformation 4(8):378-84
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
Stevenson BJ, et al.  (2008) Directed evolution of yeast pyruvate decarboxylase 1 for attenuated regulation and increased stability. Biochemistry 47(9):3013-25
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
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
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
Wei W, et al.  (2002) Solvent kinetic isotope effects monitor changes in hydrogen bonding at the active center of yeast pyruvate decarboxylase concomitant with substrate activation: the substituent at position 221 can control the state of activation. Biochemistry 41(2):451-61
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. 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
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
Killenberg-Jabs M, et al.  (1997) Role of Glu51 for cofactor binding and catalytic activity in pyruvate decarboxylase from yeast studied by site-directed mutagenesis. Biochemistry 36(7):1900-5
Norbeck J and Blomberg A  (1995) Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides. Electrophoresis 16(1):149-56
Baburina I, et al.  (1994) Substrate activation of brewers' yeast pyruvate decarboxylase is abolished by mutation of cysteine 221 to serine. Biochemistry 33(18):5630-5
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
Dyda F, et al.  (1990) Preliminary crystallographic data for the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from brewers' yeast. J Biol Chem 265(29):17413-5
Green JB  (1989) Pyruvate decarboxylase is like acetolactate synthase (ILV2) and not like the pyruvate dehydrogenase E1 subunit. FEBS Lett 246(1-2):1-5