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Identification
NamePyruvate decarboxylase isozyme 2
SynonymsNot Available
Gene NamePDC5
Enzyme Class
Biological Properties
General FunctionInvolved in magnesium ion binding
Specific FunctionSecond most abundant 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
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
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
cation binding
Process
Not Available
Gene Properties
Chromosome Locationchromosome 12
LocusYLR134W
Gene Sequence>1692 bp ATGTCTGAAATAACCTTAGGTAAATATTTATTTGAAAGATTGAGCCAAGTCAACTGTAAC ACCGTCTTCGGTTTGCCAGGTGACTTTAACTTGTCTCTTTTGGATAAGCTTTATGAAGTC AAAGGTATGAGATGGGCTGGTAACGCTAACGAATTGAACGCTGCCTATGCTGCTGATGGT TACGCTCGTATCAAGGGTATGTCCTGTATTATTACCACCTTCGGTGTTGGTGAATTGTCT GCTTTGAATGGTATTGCCGGTTCTTACGCTGAACATGTCGGTGTTTTGCACGTTGTTGGT GTTCCATCCATCTCTTCTCAAGCTAAGCAATTGTTGTTGCATCATACCTTGGGTAACGGT GACTTCACTGTTTTCCACAGAATGTCTGCCAACATTTCTGAAACCACTGCCATGATCACT GATATTGCTAACGCTCCAGCTGAAATTGACAGATGTATCAGAACCACCTACACTACCCAA AGACCAGTCTACTTGGGTTTGCCAGCTAACTTGGTTGACTTGAACGTCCCAGCCAAGTTA TTGGAAACTCCAATTGACTTGTCTTTGAAGCCAAACGACGCTGAAGCTGAAGCTGAAGTT GTTAGAACTGTTGTTGAATTGATCAAGGATGCTAAGAACCCAGTTATCTTGGCTGATGCT TGTGCTTCTAGACATGATGTCAAGGCTGAAACTAAGAAGTTGATGGACTTGACTCAATTC CCAGTTTACGTCACCCCAATGGGTAAGGGTGCTATTGACGAACAACACCCAAGATACGGT GGTGTTTACGTTGGTACCTTGTCTAGACCAGAAGTTAAGAAGGCTGTAGAATCTGCTGAT TTGATATTGTCTATCGGTGCTTTGTTGTCTGATTTCAATACCGGTTCTTTCTCTTACTCC TACAAGACCAAAAATATCGTTGAATTCCACTCTGACCACATCAAGATCAGAAACGCCACC TTCCCAGGTGTTCAAATGAAATTTGCCTTGCAAAAATTGTTGGATGCTATTCCAGAAGTC GTCAAGGACTACAAACCTGTTGCTGTCCCAGCTAGAGTTCCAATTACCAAGTCTACTCCA GCTAACACTCCAATGAAGCAAGAATGGATGTGGAACCATTTGGGTAACTTCTTGAGAGAA GGTGATATTGTTATTGCTGAAACCGGTACTTCCGCCTTCGGTATTAACCAAACTACTTTC CCAACAGATGTATACGCTATCGTCCAAGTCTTGTGGGGTTCCATTGGTTTCACAGTCGGC GCTCTATTGGGTGCTACTATGGCCGCTGAAGAACTTGATCCAAAGAAGAGAGTTATTTTA TTCATTGGTGACGGTTCTCTACAATTGACTGTTCAAGAAATCTCTACCATGATTAGATGG GGTTTGAAGCCATACATTTTTGTCTTGAATAACAACGGTTACACCATTGAAAAATTGATT CACGGTCCTCATGCCGAATATAATGAAATTCAAGGTTGGGACCACTTGGCCTTATTGCCA ACTTTTGGTGCTAGAAACTACGAAACCCACAGAGTTGCTACCACTGGTGAATGGGAAAAG TTGACTCAAGACAAGGACTTCCAAGACAACTCTAAGATTAGAATGATTGAAGTTATGTTG CCAGTCTTTGATGCTCCACAAAACTTGGTTAAACAAGCTCAATTGACTGCCGCTACTAAC GCTAAACAATAA
Protein Properties
Pfam Domain Function
Protein Residues563
Protein Molecular Weight61911.60156
Protein Theoretical pI6.4
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Pyruvate decarboxylase isozyme 2 MSEITLGKYLFERLSQVNCNTVFGLPGDFNLSLLDKLYEVKGMRWAGNANELNAAYAADG YARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNG DFTVFHRMSANISETTAMITDIANAPAEIDRCIRTTYTTQRPVYLGLPANLVDLNVPAKL LETPIDLSLKPNDAEAEAEVVRTVVELIKDAKNPVILADACASRHDVKAETKKLMDLTQF PVYVTPMGKGAIDEQHPRYGGVYVGTLSRPEVKKAVESADLILSIGALLSDFNTGSFSYS YKTKNIVEFHSDHIKIRNATFPGVQMKFALQKLLDAIPEVVKDYKPVAVPARVPITKSTP ANTPMKQEWMWNHLGNFLREGDIVIAETGTSAFGINQTTFPTDVYAIVQVLWGSIGFTVG ALLGATMAAEELDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYIFVLNNNGYTIEKLI HGPHAEYNEIQGWDHLALLPTFGARNYETHRVATTGEWEKLTQDKDFQDNSKIRMIEVML PVFDAPQNLVKQAQLTAATNAKQ
References
External Links
ResourceLink
Saccharomyces Genome Database PDC5
Uniprot IDP16467
Uniprot NamePDC5_YEAST
GenBank Gene IDU53881
Genebank Protein ID1256902
General Reference
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  • Iding, H., Siegert, P., Mesch, K., Pohl, M. (1998). "Application of alpha-keto acid decarboxylases in biotransformations." Biochim Biophys Acta 1385:307-322.9655924
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  • 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
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  • 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
  • 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
  • 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
  • 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
  • Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D., Gygi, S. P. (2003). "A proteomics approach to understanding protein ubiquitination." Nat Biotechnol 21:921-926.12872131