Literature summary for 2.7.11.4 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.

Search for more literature for 2.7.11.4

Inhibitors

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Oryctolagus cuniculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	-	Oryctolagus cuniculus	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate	-	?
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]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Oryctolagus cuniculus

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Release 2023.1 (January 2023)