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Pyruvate decarboxylase isozyme 3 (P26263)

Identification
NamePyruvate decarboxylase isozyme 3
SynonymsNot Available
Gene NamePDC6
Enzyme Class
Biological Properties
General FunctionInvolved in magnesium ion binding
Specific FunctionMinor 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-keto-acids) 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. The expression level of this protein in the presence of fermentable carbon sources is so low that it can not compensate for the other two pyruvate decarboxylases to sustain fermentation
Cellular LocationCytoplasm
SMPDB Pathways
Ethanol fermentationPW002448 ThumbThumb?image type=greyscaleThumb?image type=simple
Isoleucine degradationPW002491 ThumbThumb?image type=greyscaleThumb?image type=simple
Phenylalanine metabolismPW002437 ThumbThumb?image type=greyscaleThumb?image type=simple
Pyruvate metabolismPW002447 ThumbThumb?image type=greyscaleThumb?image type=simple
Tryptophan metabolismPW002442 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 + hydron → Carbon dioxide + Phenylacetaldehyde
(4-hydroxyphenyl)pyruvic acid + hydron → 4-Hydroxyphenylacetaldehyde + Carbon dioxide
3-(indol-3-yl)pyruvate + hydron → Indoleacetaldehyde + Carbon dioxide
Pyruvic acid + hydron → Carbon dioxide + Acetaldehyde
Alpha-Ketoisovaleric acid + hydron → Carbon dioxide + isobutyraldehyde
KEGG Reactions
Pyruvic acid + hydron → Carbon dioxide + Acetaldehyde
Pyruvic acid + Acetaldehyde + hydron → Carbon dioxide + (R)-Acetoin
Metabolites
YMDB IDNameView
YMDB00022AcetaldehydeShow
YMDB00039(S)-2-Aceto-2-hydroxybutanoic acidShow
YMDB000712-Ketobutyric acidShow
YMDB00116PhenylacetaldehydeShow
YMDB00168(S)-3-methyl-2-oxovaleric acidShow
YMDB001693-(indol-3-yl)pyruvic acidShow
YMDB00175Pyruvic acidShow
YMDB00177(S)-2-AcetolactateShow
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
cation binding
metal ion binding
vitamin binding
magnesium ion binding
thiamin pyrophosphate binding
catalytic activity
transferase activity
lyase activity
carbon-carbon lyase activity
carboxy-lyase activity
binding
ion binding
Process
Not Available
Gene Properties
Chromosome Locationchromosome 7
LocusYGR087C
Gene Sequence>1692 bp ATGTCTGAAATTACTCTTGGAAAATACTTATTTGAAAGATTGAAGCAAGTTAATGTTAAC ACCATTTTTGGGCTACCAGGCGACTTCAACTTGTCCCTATTGGACAAGATTTACGAGGTA GATGGATTGAGATGGGCTGGTAATGCAAATGAGCTGAACGCCGCCTATGCCGCCGATGGT TACGCACGCATCAAGGGTTTATCTGTGCTGGTAACTACTTTTGGCGTAGGTGAATTATCC GCCTTGAATGGTATTGCAGGATCGTATGCAGAACACGTCGGTGTACTGCATGTTGTTGGT GTCCCCTCTATCTCCGCTCAGGCTAAGCAATTGTTGTTGCATCATACCTTGGGTAACGGT GATTTTACCGTTTTTCACAGAATGTCCGCCAATATCTCAGAAACTACATCAATGATTACA GACATTGCTACAGCCCCTTCAGAAATCGATAGGTTGATCAGGACAACATTTATAACACAA AGGCCTAGCTACTTGGGGTTGCCAGCGAATTTGGTAGATCTAAAGGTTCCTGGTTCTCTT TTGGAAAAACCGATTGATCTATCATTAAAACCTAACGATCCCGAAGCTGAAAAGGAAGTT ATTGATACCGTACTAGAATTGATCCAGAATTCGAAAAACCCTGTTATACTATCGGATGCC TGTGCTTCTAGGCACAACGTTAAAAAAGAAACCCAGAAGTTAATTGATTTGACGCAATTC CCAGCTTTTGTGACACCTCTAGGTAAAGGGTCAATAGATGAACAGCATCCCAGATATGGC GGTGTTTATGTGGGAACGCTGTCCAAACAAGACGTGAAACAGGCCGTTGAGTCGGCTGAT TTGATCCTTTCGGTCGGTGCTTTGCTCTCTGATTTTAACACAGGTTCGTTTTCCTACTCC TACAAGACTAAAAATGTAGTGGAGTTTCATTCCGATTACGTAAAGGTGAAGAACGCTACG TTCCTCGGTGTACAAATGAAATTTGCACTACAAAACTTACTGAAGGTTATTCCCGATGTT GTTAAGGGCTACAAGAGCGTTCCCGTACCAACCAAAACTCCCGCAAACAAAGGTGTACCT GCTAGCACGCCCTTGAAACAAGAGTGGTTGTGGAACGAATTGTCCAAATTCTTGCAAGAA GGTGATGTTATCATTTCCGAGACCGGCACGTCTGCCTTCGGTATCAATCAAACTATCTTT CCTAAGGACGCCTACGGTATCTCGCAGGTGTTGTGGGGGTCCATCGGTTTTACAACAGGA GCAACTTTAGGTGCTGCCTTTGCCGCTGAGGAGATTGACCCCAACAAGAGAGTCATCTTA TTCATAGGTGACGGGTCTTTGCAGTTAACCGTCCAAGAAATCTCCACCATGATCAGATGG GGGTTAAAGCCGTATCTTTTTGTCCTTAACAACGACGGCTACACTATCGAAAAGCTGATT CATGGGCCTCACGCAGAGTACAACGAAATCCAGACCTGGGATCACCTCGCCCTGTTGCCC GCATTTGGTGCGAAAAAGTACGAAAATCACAAGATCGCCACTACGGGTGAGTGGGATGCC TTAACCACTGATTCAGAGTTCCAGAAAAACTCGGTGATCAGACTAATTGAACTGAAACTG CCCGTCTTTGATGCTCCGGAAAGTTTGATCAAACAAGCGCAATTGACTGCCGCTACAAAT GCCAAACAATAA
Protein Properties
Pfam Domain Function
Protein Residues563
Protein Molecular Weight61579.89844
Protein Theoretical pI6.11
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Pyruvate decarboxylase isozyme 3 MSEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADG YARIKGLSVLVTTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNG DFTVFHRMSANISETTSMITDIATAPSEIDRLIRTTFITQRPSYLGLPANLVDLKVPGSL LEKPIDLSLKPNDPEAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDLTQF PAFVTPLGKGSIDEQHPRYGGVYVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYS YKTKNVVEFHSDYVKVKNATFLGVQMKFALQNLLKVIPDVVKGYKSVPVPTKTPANKGVP ASTPLKQEWLWNELSKFLQEGDVIISETGTSAFGINQTIFPKDAYGISQVLWGSIGFTTG ATLGAAFAAEEIDPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLI HGPHAEYNEIQTWDHLALLPAFGAKKYENHKIATTGEWDALTTDSEFQKNSVIRLIELKL PVFDAPESLIKQAQLTAATNAKQ
References
External Links
ResourceLink
Saccharomyces Genome Database PDC6
Uniprot IDP26263
Uniprot NamePDC6_YEAST
GenBank Gene IDX55905
Genebank Protein ID4116
General Reference
  • Hohmann, S. (1991). "Characterization of PDC6, a third structural gene for pyruvate decarboxylase in Saccharomyces cerevisiae." J Bacteriol 173:7963-7969.1744053
  • Tettelin, H., Agostoni Carbone, M. L., Albermann, K., Albers, M., Arroyo, J., Backes, U., Barreiros, T., Bertani, I., Bjourson, A. J., Bruckner, M., Bruschi, C. V., Carignani, G., Castagnoli, L., Cerdan, E., Clemente, M. L., Coblenz, A., Coglievina, M., Coissac, E., Defoor, E., Del Bino, S., Delius, H., Delneri, D., de Wergifosse, P., Dujon, B., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Nature 387:81-84.9169869
  • 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
  • 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
  • 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