|
P26263
|
Pyruvate decarboxylase isozyme 3 |
Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6)implicated in the nonoxidative conversion of pyruvate to acetaldehydeand carbon dioxide during alcoholic fermentation. Most of the producedacetaldehyde is subsequently reduced to ethanol, but some is requiredfor cytosolic acetyl-CoA production for biosynthetic pathways. Theenzyme 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 acidcatabolism. Here the enzyme catalyzes the decarboxylation of aminoacids, which, in a first step, have been transaminated to thecorresponding 2-oxo acids. In a third step, the resulting aldehydes arereduced to alcohols, collectively referred to as fusel oils oralcohols. Its preferred substrates are the transaminated amino acidsderived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate),valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate),isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate.In a side-reaction the carbanionic intermediate (or active aldehyde)generated by decarboxylation or by activation of an aldehyde can reactwith an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level ofthis protein in the presence of fermentable carbon sources is so lowthat it cannot compensate for the other two pyruvate decarboxylases tosustain fermentation. |
YGR087C |
Saccharomyces cerevisiae |
RSY113 |
20559436
|
|
P26263
|
Pyruvate decarboxylase isozyme 3 |
Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6)implicated in the nonoxidative conversion of pyruvate to acetaldehydeand carbon dioxide during alcoholic fermentation. Most of the producedacetaldehyde is subsequently reduced to ethanol, but some is requiredfor cytosolic acetyl-CoA production for biosynthetic pathways. Theenzyme 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 acidcatabolism. Here the enzyme catalyzes the decarboxylation of aminoacids, which, in a first step, have been transaminated to thecorresponding 2-oxo acids. In a third step, the resulting aldehydes arereduced to alcohols, collectively referred to as fusel oils oralcohols. Its preferred substrates are the transaminated amino acidsderived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate),valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate),isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate.In a side-reaction the carbanionic intermediate (or active aldehyde)generated by decarboxylation or by activation of an aldehyde can reactwith an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level ofthis protein in the presence of fermentable carbon sources is so lowthat it cannot compensate for the other two pyruvate decarboxylases tosustain fermentation. |
YGR087C |
Saccharomyces cerevisiae |
RSY255 |
20559436
|
|
P26263
|
Pyruvate decarboxylase isozyme 3 |
Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6)implicated in the nonoxidative conversion of pyruvate to acetaldehydeand carbon dioxide during alcoholic fermentation. Most of the producedacetaldehyde is subsequently reduced to ethanol, but some is requiredfor cytosolic acetyl-CoA production for biosynthetic pathways. Theenzyme 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 acidcatabolism. Here the enzyme catalyzes the decarboxylation of aminoacids, which, in a first step, have been transaminated to thecorresponding 2-oxo acids. In a third step, the resulting aldehydes arereduced to alcohols, collectively referred to as fusel oils oralcohols. Its preferred substrates are the transaminated amino acidsderived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate),valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate),isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate.In a side-reaction the carbanionic intermediate (or active aldehyde)generated by decarboxylation or by activation of an aldehyde can reactwith an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level ofthis protein in the presence of fermentable carbon sources is so lowthat it cannot compensate for the other two pyruvate decarboxylases tosustain fermentation. |
YGR087C |
Saccharomyces cerevisiae |
RSY782 |
20559436
|
|
P26263
|
Pyruvate decarboxylase isozyme 3 |
Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6)implicated in the nonoxidative conversion of pyruvate to acetaldehydeand carbon dioxide during alcoholic fermentation. Most of the producedacetaldehyde is subsequently reduced to ethanol, but some is requiredfor cytosolic acetyl-CoA production for biosynthetic pathways. Theenzyme 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 acidcatabolism. Here the enzyme catalyzes the decarboxylation of aminoacids, which, in a first step, have been transaminated to thecorresponding 2-oxo acids. In a third step, the resulting aldehydes arereduced to alcohols, collectively referred to as fusel oils oralcohols. Its preferred substrates are the transaminated amino acidsderived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate),valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate),isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate.In a side-reaction the carbanionic intermediate (or active aldehyde)generated by decarboxylation or by activation of an aldehyde can reactwith an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level ofthis protein in the presence of fermentable carbon sources is so lowthat it cannot compensate for the other two pyruvate decarboxylases tosustain fermentation. |
YGR087C |
Saccharomyces cerevisiae |
RSY954 |
20559436
|
|
P26263
|
Pyruvate decarboxylase isozyme 3 |
Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6)implicated in the nonoxidative conversion of pyruvate to acetaldehydeand carbon dioxide during alcoholic fermentation. Most of the producedacetaldehyde is subsequently reduced to ethanol, but some is requiredfor cytosolic acetyl-CoA production for biosynthetic pathways. Theenzyme 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 acidcatabolism. Here the enzyme catalyzes the decarboxylation of aminoacids, which, in a first step, have been transaminated to thecorresponding 2-oxo acids. In a third step, the resulting aldehydes arereduced to alcohols, collectively referred to as fusel oils oralcohols. Its preferred substrates are the transaminated amino acidsderived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate),valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate),isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate.In a side-reaction the carbanionic intermediate (or active aldehyde)generated by decarboxylation or by activation of an aldehyde can reactwith an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level ofthis protein in the presence of fermentable carbon sources is so lowthat it cannot compensate for the other two pyruvate decarboxylases tosustain fermentation. |
YGR087C |
Saccharomyces cerevisiae |
SEY6210 |
20559436
|
|
P26263
|
Pyruvate decarboxylase isozyme 3 |
Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6)implicated in the nonoxidative conversion of pyruvate to acetaldehydeand carbon dioxide during alcoholic fermentation. Most of the producedacetaldehyde is subsequently reduced to ethanol, but some is requiredfor cytosolic acetyl-CoA production for biosynthetic pathways. Theenzyme 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 acidcatabolism. Here the enzyme catalyzes the decarboxylation of aminoacids, which, in a first step, have been transaminated to thecorresponding 2-oxo acids. In a third step, the resulting aldehydes arereduced to alcohols, collectively referred to as fusel oils oralcohols. Its preferred substrates are the transaminated amino acidsderived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate),valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate),isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate.In a side-reaction the carbanionic intermediate (or active aldehyde)generated by decarboxylation or by activation of an aldehyde can reactwith an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level ofthis protein in the presence of fermentable carbon sources is so lowthat it cannot compensate for the other two pyruvate decarboxylases tosustain fermentation. |
YGR087C |
Saccharomyces cerevisiae |
SF264-1D |
20559436
|
|
P26263
|
Pyruvate decarboxylase isozyme 3 |
Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6)implicated in the nonoxidative conversion of pyruvate to acetaldehydeand carbon dioxide during alcoholic fermentation. Most of the producedacetaldehyde is subsequently reduced to ethanol, but some is requiredfor cytosolic acetyl-CoA production for biosynthetic pathways. Theenzyme 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 acidcatabolism. Here the enzyme catalyzes the decarboxylation of aminoacids, which, in a first step, have been transaminated to thecorresponding 2-oxo acids. In a third step, the resulting aldehydes arereduced to alcohols, collectively referred to as fusel oils oralcohols. Its preferred substrates are the transaminated amino acidsderived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate),valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate),isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate.In a side-reaction the carbanionic intermediate (or active aldehyde)generated by decarboxylation or by activation of an aldehyde can reactwith an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level ofthis protein in the presence of fermentable carbon sources is so lowthat it cannot compensate for the other two pyruvate decarboxylases tosustain fermentation. |
YGR087C |
Saccharomyces cerevisiae |
Snf7 |
20559436
|
|
P26263
|
Pyruvate decarboxylase isozyme 3 |
Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6)implicated in the nonoxidative conversion of pyruvate to acetaldehydeand carbon dioxide during alcoholic fermentation. Most of the producedacetaldehyde is subsequently reduced to ethanol, but some is requiredfor cytosolic acetyl-CoA production for biosynthetic pathways. Theenzyme 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 acidcatabolism. Here the enzyme catalyzes the decarboxylation of aminoacids, which, in a first step, have been transaminated to thecorresponding 2-oxo acids. In a third step, the resulting aldehydes arereduced to alcohols, collectively referred to as fusel oils oralcohols. Its preferred substrates are the transaminated amino acidsderived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate),valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate),isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate.In a side-reaction the carbanionic intermediate (or active aldehyde)generated by decarboxylation or by activation of an aldehyde can reactwith an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level ofthis protein in the presence of fermentable carbon sources is so lowthat it cannot compensate for the other two pyruvate decarboxylases tosustain fermentation. |
YGR087C |
Saccharomyces cerevisiae |
VPS23 |
20559436
|