Literature summary for 1.8.1.4 extracted from

Park, Y.H.; Patel, M.S.
Characterization of interactions of dihydrolipoamide dehydrogenase with its binding protein in the human pyruvate dehydrogenase complex (2010), Biochem. Biophys. Res. Commun., 395, 416-419 .

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Protein Variants

Protein Variants	Comment	Organism
D413A	substitutions has no large effects on E3 activity when measured in its free form. However, when reconstituted in the complex, the pyruvate dehydrogenase activity is reduced to 18%. The binding affinities of the mutant to the di-domain of the E3-binding protein are severely reduced	Homo sapiens
Y438A	substitutions has no large effects on E3 activity when measured in its free form. However, when reconstituted in the complex, the pyruvate dehydrogenase activity is reduced to 9%. The binding affinities of the mutant to the di-domain of the E3-binding protein are severely reduced and binding of is accompanied by an unfavorable enthalpy change and a large positive entropy change	Homo sapiens
Y438H	substitutions has no large effects on E3 activity when measured in its free form. However, when reconstituted in the complex, the pyruvate dehydrogenase activity is reduced to 20%. The binding affinities of the mutant to the di-domain of the E3-binding protein ire severely reduced	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P09622	dihydrolipoyl dehydrogenase, i.e. E3 subunit of pyruvate dehydrogenase complex, cf. EC 1.2.1.104	-

Synonyms

Synonyms	Comment	Organism
DLD	-	Homo sapiens

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Release 2023.1 (January 2023)