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Literature summary for 3.1.3.52 extracted from

  • Bradford, A.P.; Cook, K.G.; Yeaman, S.J.
    Control of branched-chain 2-oxo acid dehydrogenase complex by reversible phosphorylation (1985), Biochem. Soc. Trans., 13, 745-746.
No PubMed abstract available
Search for more literature for 3.1.3.52

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
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 Bos taurus 5739
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate + H2O Bos taurus role in breakdown of essential branched-chain amino acids [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] + phosphate
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 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate + H2O catalyzes the release of phosphate from both sites on the alpha-subunit of the branched-chain 2-oxo acid dehydrogenase E1 component, which results in reactivation of the complex Bos taurus [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] + phosphate
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 ?
[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate + H2O role in breakdown of essential branched-chain amino acids Bos taurus [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] + phosphate
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 ?

Subunits

Subunits Comment Organism
dimer alpha,beta Bos taurus