Literature summary for 1.2.4.4 extracted from

Brautigam, C.A.; Wynn, R.M.; Chuang, J.L.; Naik, M.T.; Young, B.B.; Huang, T.H.; Chuang, D.T.
Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex (2011), J. Biol. Chem., 286, 23476-23488.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	branched-chain alpha-keto acid dehydrogenase complex is essentially devoid of the constituent dihydrolipoamide dehydrogenase component (E3). The absence of E3 is associated with the low affinity of the subunit-binding domain of human BCKDC for hE3	Homo sapiens	?	-	?

Synonyms

Synonyms	Comment	Organism
BCKDC	-	Homo sapiens
branched-chain alpha-ketoacid dehydrogenase complex	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
CoA	-	Homo sapiens
NAD+	-	Homo sapiens

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Release 2023.1 (January 2023)