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Literature summary extracted from

  • Harris, R.A.; Paxton, R.; DePaoli-Roach, A.
    Inhibition of branched chain alpha-ketoacid dehydrogenase kinase activity by alpha-chloroisocaproate (1982), J. Biol. Chem., 257, 13915-13918.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.2 2-Chloroisohexanoate weak Oryctolagus cuniculus
2.7.11.4 2-Chloroisohexanoate ATP does not protect; i.e. 2-chloro-4-methylpentanoate, strong Oryctolagus cuniculus
2.7.11.4 Dichloroacetate
-
 Oryctolagus cuniculus
2.7.11.4 additional information no inhibition by DL-leucine Oryctolagus cuniculus
2.7.11.4 pyruvate
-
 Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.11.2 ATP + [pyruvate dehydrogenase (lipoamide)] Oryctolagus cuniculus catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
2.7.11.4 ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] Oryctolagus cuniculus phosphorylation inactivates EC 1.2.4.4 ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.2 Oryctolagus cuniculus
-
-
-
2.7.11.4 Oryctolagus cuniculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.2 liver
-
 Oryctolagus cuniculus
-
2.7.11.4 liver
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.2 ATP + [pyruvate dehydrogenase (lipoamide)]
-
 Oryctolagus cuniculus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
2.7.11.2 ATP + [pyruvate dehydrogenase (lipoamide)] catalyzes inactivation through phosphorylation of pyruvate dehydrogenase complex EC 1.2.4.1 Oryctolagus cuniculus ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
-
 ir
2.7.11.4 ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
-
 Oryctolagus cuniculus ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
 ?
2.7.11.4 ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphorylation inactivates EC 1.2.4.4 Oryctolagus cuniculus ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.2 37
-
 assay at Oryctolagus cuniculus
2.7.11.4 37
-
 assay at Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.2 ATP dependent on Oryctolagus cuniculus