Identification
NamePyruvate decarboxylase isozyme 1
SynonymsNot Available
Gene NamePDC1
Enzyme Class
Biological Properties
General FunctionInvolved in magnesium ion binding
Specific FunctionMajor of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins
Cellular LocationCytoplasm. Nucleus
SMPDB Pathways
Tyrosine metabolismPW002441 ThumbThumb?image type=greyscaleThumb?image type=simple
Valine DegradationPW002489 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Glycolysis / Gluconeogenesisec00010 Map00010
Phenylalanine metabolismec00360 Map00360
Pyruvate metabolismec00620 Map00620
Tryptophan metabolismec00380 Map00380
Tyrosine metabolismec00350 Map00350
SMPDB Reactions
keto-phenylpyruvic acid + hydronCarbon dioxide + Phenylacetaldehyde
(4-hydroxyphenyl)pyruvic acid + hydron4-Hydroxyphenylacetaldehyde + Carbon dioxide
3-(indol-3-yl)pyruvate + hydronIndoleacetaldehyde + Carbon dioxide
Pyruvic acid + hydronCarbon dioxide + Acetaldehyde
Alpha-Ketoisovaleric acid + hydronCarbon dioxide + isobutyraldehyde
KEGG Reactions
Pyruvic acid + hydronCarbon dioxide + Acetaldehyde
Pyruvic acid + Acetaldehyde + hydronCarbon dioxide + (R)-Acetoin
Metabolites
YMDB IDNameView
YMDB00022AcetaldehydeShow
YMDB00116PhenylacetaldehydeShow
YMDB00168(S)-3-methyl-2-oxovaleric acidShow
YMDB001693-(indol-3-yl)pyruvic acidShow
YMDB00175Pyruvic acidShow
YMDB00354IndoleacetaldehydeShow
YMDB00365Alpha-Ketoisovaleric acidShow
YMDB00410(R)-AcetoinShow
YMDB00482isobutyraldehydeShow
YMDB004852-MethylbutanalShow
YMDB00786keto-phenylpyruvic acidShow
YMDB00862hydronShow
YMDB00912Carbon dioxideShow
YMDB00958(4-hydroxyphenyl)pyruvic acidShow
YMDB010693-(indol-3-yl)pyruvateShow
YMDB161644-HydroxyphenylacetaldehydeShow
GO Classification
Component
Not Available
Function
carboxy-lyase activity
binding
ion binding
cation binding
metal ion binding
vitamin binding
magnesium ion binding
thiamin pyrophosphate binding
catalytic activity
transferase activity
lyase activity
carbon-carbon lyase activity
Process
Not Available
Gene Properties
Chromosome Locationchromosome 12
LocusYLR044C
Gene Sequence>1692 bp ATGTCTGAAATTACTTTGGGTAAATATTTGTTCGAAAGATTAAAGCAAGTCAACGTTAAC ACCGTTTTCGGTTTGCCAGGTGACTTCAACTTGTCCTTGTTGGACAAGATCTACGAAGTT GAAGGTATGAGATGGGCTGGTAACGCCAACGAATTGAACGCTCGTTACGCCGCTGATGGT TACGCTCGTATCAAGGGTATGTCTTGTATCATCACCACCTTCGGTGTCGGTGAATTGTCT GCTTTGAACGGTATTGCCGGTTCTTACGCTGAACACGTCGGTGTTTTGCACGTTGTTGGT GTCCCATCCATCTCTTCTCAAGCTAAGCAATTGTTGTTGCACCACACCTTGGGTAACGGT GACTTCACTGTTTTCCACAGAATGTCTGCCAACATTTCTGAAACCACTGCTATGATCACT GACATCTGTACCGCCCCAGCTGAAATTGACAGATGTATCAGAACCACTTACGTCACCCAA AGACCAGTCTACTTAGGTTTGCCAGCTAACTTGGTCGACTTGAACGTCCCAGCTAAGTTG TTGCAAACTCCAATTGACATGTCTTTGAAGCCAAACGATGCTGAATCCGAAAAGGAAGTC ATTGACACCATCTTGGTCTTGGCTAAGGATGCTAAGAACCCAGTTATCTTGGCTGATGCT TGTTGTTCCAGACACGACGTCAAGGCTGAAACTAAGAAGTTGATTGACTTGACTCAATTC CCAGCTTTCGTCACCCCAATGGGTAAGGGTTCCATTAGCGAACAACACCCAAGATACGGT GGTGTTTACGTCGGTACCTTGTCCAAGCCAGAAGTTAAGGAAGCCGTTGAATCTGCTGAC TTGATTTTGTCTGTCGGTGCTTTGTTGTCTGATTTCAACACCGGTTCTTTCTCTTACTCT TACAAGACCAAGAACATTGTCGAATTCCACTCCGACCACATGAAGATCAGAAACGCCACT TTCCCAGGTGTCCAAATGAAATTCGTTTTGCAAAAGTTGTTGACCAATATTGCTGACGCC GCTAAGGGTTACAAGCCAGTTGCTGTCCCAGCTAGAACTCCAGCTAACGCTGCTGTCCCA GCTTCTACCCCATTGAAGCAAGAATGGATGTGGAACCAATTGGGTAACTTCTTGCAAGAA GGTGATGTTGTCATTGCTGAAACCGGTACCTCCGCTTTCGGTATCAACCAAACCACTTTC CCAAACAACACCTACGGTATCTCTCAAGTCTTATGGGGTTCCATTGGTTTCACCACTGGT GCTACCTTGGGTGCTGCTTTCGCTGCTGAAGAAATTGATCCAAAGAAGAGAGTTATCTTA TTCATTGGTGACGGTTCTTTGCAATTGACTGTTCAAGAAATCTCCACCATGATCAGATGG GGCTTGAAGCCATACTTGTTCGTCTTGAACAACGATGGTTACACCATTGAAAAGTTGATT CACGGTCCAAAGGCTCAATACAACGAAATTCAAGGTTGGGACCACCTATCCTTGTTGCCA ACTTTCGGTGCTAAGGACTACGAAACCCACAGAGTCGCTACCACCGGTGAATGGGACAAG TTGACCCAAGACAAGTCTTTCAACGACAACTCTAAGATCAGAATGATTGAGGTTATGTTG CCAGTCTTCGATGCTCCACAAAACTTGGTTGAACAAGCTAAGTTGACTGCTGCTACCAAC GCTAAGCAATAA
Protein Properties
Pfam Domain Function
Protein Residues563
Protein Molecular Weight61494.89844
Protein Theoretical pI6.11
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Pyruvate decarboxylase isozyme 1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADG YARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNG DFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGLPANLVDLNVPAKL LQTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQF PAFVTPMGKGSIDEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYS YKTKNIVEFHSDHMKIRNATFPGVQMKFVLQKLLTTIADAAKGYKPVAVPARTPANAAVP ASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQVLWGSIGFTTG ATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLI HGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVATTGEWDKLTQDKSFNDNSKIRMIEIML PVFDAPQNLVEQAKLTAATNAKQ
References
External Links
ResourceLink
Saccharomyces Genome Database PDC1
Uniprot IDP06169
Uniprot NamePDC1_YEAST
GenBank Gene IDX77316
Genebank Protein ID871533
PDB ID
1QPB
General Reference
  • Kellermann, E., Seeboth, P. G., Hollenberg, C. P. (1986). "Analysis of the primary structure and promoter function of a pyruvate decarboxylase gene (PDC1) from Saccharomyces cerevisiae." Nucleic Acids Res 14:8963-8977.3537965
  • Hohmann, S., Cederberg, H. (1990). "Autoregulation may control the expression of yeast pyruvate decarboxylase structural genes PDC1 and PDC5." Eur J Biochem 188:615-621.2185016
  • Johnston, M., Hillier, L., Riles, L., Albermann, K., Andre, B., Ansorge, W., Benes, V., Bruckner, M., Delius, H., Dubois, E., Dusterhoft, A., Entian, K. D., Floeth, M., Goffeau, A., Hebling, U., Heumann, K., Heuss-Neitzel, D., Hilbert, H., Hilger, F., Kleine, K., Kotter, P., Louis, E. J., Messenguy, F., Mewes, H. W., Hoheisel, J. D., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Nature 387:87-90.9169871
  • Garrels, J. I., Futcher, B., Kobayashi, R., Latter, G. I., Schwender, B., Volpe, T., Warner, J. R., McLaughlin, C. S. (1994). "Protein identifications for a Saccharomyces cerevisiae protein database." Electrophoresis 15:1466-1486.7895733
  • Norbeck, J., 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 16:149-156.7737086
  • Lehmann, H., Fischer, G., Hubner, G., Kohnert, K. D., Schellenberger, A. (1973). "The influence of steric and electronic parameters on the substrate behavior of -oxo acids to yeast pyruvate decarboxylase." Eur J Biochem 32:83-87.4687392
  • Schmitt, H. D., Zimmermann, F. K. (1982). "Genetic analysis of the pyruvate decarboxylase reaction in yeast glycolysis." J Bacteriol 151:1146-1152.7050079
  • Liesen, T., Hollenberg, C. P., Heinisch, J. J. (1996). "ERA, a novel cis-acting element required for autoregulation and ethanol repression of PDC1 transcription in Saccharomyces cerevisiae." Mol Microbiol 21:621-632.8866484
  • Garrels, J. I., McLaughlin, C. S., Warner, J. R., Futcher, B., Latter, G. I., Kobayashi, R., Schwender, B., Volpe, T., Anderson, D. S., Mesquita-Fuentes, R., Payne, W. E. (1997). "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Electrophoresis 18:1347-1360.9298649
  • Dickinson, J. R., Lanterman, M. M., Danner, D. J., Pearson, B. M., Sanz, P., Harrison, S. J., Hewlins, M. J. (1997). "A 13C nuclear magnetic resonance investigation of the metabolism of leucine to isoamyl alcohol in Saccharomyces cerevisiae." J Biol Chem 272:26871-26878.9341119
  • Dickinson, J. R., Harrison, S. J., Hewlins, M. J. (1998). "An investigation of the metabolism of valine to isobutyl alcohol in Saccharomyces cerevisiae." J Biol Chem 273:25751-25756.9748245
  • Flikweert, M. T., de Swaaf, M., van Dijken, J. P., Pronk, J. T. (1999). "Growth requirements of pyruvate-decarboxylase-negative Saccharomyces cerevisiae." FEMS Microbiol Lett 174:73-79.10234824
  • Eberhardt, I., Cederberg, H., Li, H., Konig, S., Jordan, F., Hohmann, S. (1999). "Autoregulation of yeast pyruvate decarboxylase gene expression requires the enzyme but not its catalytic activity." Eur J Biochem 262:191-201.10231381
  • Polevoda, B., Norbeck, J., Takakura, H., Blomberg, A., Sherman, F. (1999). "Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae." EMBO J 18:6155-6168.10545125
  • Dickinson, J. R., Harrison, S. J., Dickinson, J. A., Hewlins, M. J. (2000). "An investigation of the metabolism of isoleucine to active Amyl alcohol in Saccharomyces cerevisiae." J Biol Chem 275:10937-10942.10753893
  • Neuser, F., Zorn, H., Berger, R. G. (2000). "Generation of odorous acyloins by yeast pyruvate decarboxylases and their occurrence in sherry and soy sauce." J Agric Food Chem 48:6191-6195.11141278
  • Dickinson, J. R., Salgado, L. E., Hewlins, M. J. (2003). "The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae." J Biol Chem 278:8028-8034.12499363
  • Vuralhan, Z., Morais, M. A., Tai, S. L., Piper, M. D., Pronk, J. T. (2003). "Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae." Appl Environ Microbiol 69:4534-4541.12902239
  • Iding, H., Siegert, P., Mesch, K., Pohl, M. (1998). "Application of alpha-keto acid decarboxylases in biotransformations." Biochim Biophys Acta 1385:307-322.9655924
  • Hohmann, S., Meacock, P. A. (1998). "Thiamin metabolism and thiamin diphosphate-dependent enzymes in the yeast Saccharomyces cerevisiae: genetic regulation." Biochim Biophys Acta 1385:201-219.9655908
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Li, X., Gerber, S. A., Rudner, A. D., Beausoleil, S. A., Haas, W., Villen, J., Elias, J. E., Gygi, S. P. (2007). "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." J Proteome Res 6:1190-1197.17330950
  • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Proc Natl Acad Sci U S A 104:2193-2198.17287358
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
  • Dyda, F., Furey, W., Swaminathan, S., Sax, M., Farrenkopf, B., Jordan, F. (1993). "Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-A resolution." Biochemistry 32:6165-6170.8512926
  • Arjunan, P., Umland, T., Dyda, F., Swaminathan, S., Furey, W., Sax, M., Farrenkopf, B., Gao, Y., Zhang, D., Jordan, F. (1996). "Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution." J Mol Biol 256:590-600.8604141
  • Lu, G., Dobritzsch, D., Baumann, S., Schneider, G., Konig, S. (2000). "The structural basis of substrate activation in yeast pyruvate decarboxylase. A crystallographic and kinetic study." Eur J Biochem 267:861-868.10651824