Literature summary for 1.2.1.104 extracted from

Guo, J.; Hezaveh, S.; Tatur, J.; Zeng, A.P.; Jandt, U.
Reengineering of the human pyruvate dehydrogenase complex from disintegration to highly active agglomerates (2017), Biochem. J., 474, 865-875 .

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P08559 and P11177 and O00330 and P10515 and P09622	P08559 i.e. subunit PdhA1, cf. EC 1.2.4.1, P11177 i.e. subunit PdhB1, cf. EC 1.2.4.1, O00330 i.e. subunit PdhX, P10515 i.e. subunit DlaT, cf. EC 2.3.1.12, P09622 i.e. subunit Dld, cf. EC 1.8.1.4, respectively	-

Subunits

Subunits	Comment	Organism
multimer	x * 70000, E2 subunit, x * 55000, E3 subunit, SDS-PAGE	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	disintegration of the pyruvate dehydrogenase complex core via double truncations (eight residues from E2 and seven residues from E3 binding protein PdhX) leads to the formation of highly active (approximately 70% of wild-type) unordered clusters or agglomerates and inactive nonagglomerated species (hexamer/trimer). After additional deletion of N-terminal swinging arms, the C-terminal truncations also cause the formation of agglomerates of minimized E2/E3 binding protein complexes	Homo sapiens

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Release 2023.1 (January 2023)