Literature summary for 2.7.11.4 extracted from

Hawes, J.W.; Schnepf, R.J.; Jenkins, A.E.; Shimomura, Y.; Popov, K.M.; Harris, R.A.
Roles of amino acid residues surrounding phosphorylation site 1 and branched-chain alpha-ketoacid dehydrogenase (BCKDH) in catalysis and phosphorylation site recognition by BCKDH kinase (1995), J. Biol. Chem., 270, 31071-31076.

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Inhibitors

Inhibitors	Comment	Organism	Structure
thiamine diphosphate	inhibits phosphorylation of wild-type E1, mutant E1-S303A and mutant E1-D296A/S303A, but not phosphorylation of mutant E1-H292A	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	-	Rattus norvegicus	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate	-	?
additional information	R288A mutant of E1 is not phosphorylated by the enzyme	Rattus norvegicus	?	-	?

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Release 2023.1 (January 2023)