Literature summary for 1.2.1.104 extracted from

Kyrilis, F.L.; Semchonok, D.A.; Skalidis, I.; Tueting, C.; Hamdi, F.; OReilly, F.J.; Rappsilber, J.; Kastritis, P.L.
Integrative structure of a 10-megadalton eukaryotic pyruvate dehydrogenase complex from native cell extracts (2021), Cell Rep., 34, 108727 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
asymmetric reconstruction of the active, native pyruvate dehydrogenase complex by cryo-EM as a dynamic assembly. Enzyme clusters form a transient catalytic nanocompartment. The flexible parts of the dehydrogenase factory are notably restricted by a density cloud surrounding single E1p and E3 subunits. This density cloud presumably is composed of E1p and E3. The E1p and E3 proteins are not observed to interact directly with the E2p core but are spatially confined in relative proximity	Thermochaetoides thermophila

Crystallization (Comment)

Organism

asymmetric reconstruction of the active, native pyruvate dehydrogenase complex by cryo-EM as a dynamic assembly. Enzyme clusters form a transient catalytic nanocompartment. The flexible parts of the dehydrogenase factory are notably restricted by a density cloud surrounding single E1p and E3 subunits. This density cloud presumably is composed of E1p and E3. The E1p and E3 proteins are not observed to interact directly with the E2p core but are spatially confined in relative proximity

Thermochaetoides thermophila

Organism

Organism	UniProt	Comment	Textmining
Thermochaetoides thermophila	G0SHF3 and G0RYE0	G0SHF3 i.e. E1 subunit alpha, G0RYE0 i.e. E1 subunit beta	-
Thermochaetoides thermophila DSM 1495	G0SHF3 and G0RYE0	G0SHF3 i.e. E1 subunit alpha, G0RYE0 i.e. E1 subunit beta	-

Synonyms

Synonyms	Comment	Organism
CTHT_0006350	cf. EC 1.2.4.1	Thermochaetoides thermophila
CTHT_0069820	cf. EC 1.2.4.1	Thermochaetoides thermophila
E1 component subunit alpha	-	Thermochaetoides thermophila
E1 component subunit beta	-	Thermochaetoides thermophila

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Release 2023.1 (January 2023)