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Literature summary for 1.2.4.1 extracted from

  • Chandrasekhar, K.; Arjunan, P.; Sax, M.; Nemeria, N.; Jordan, F.; Furey, W.
    Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution (2006), Acta crystallogr. Sect. D, 62, 1382-1386.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
preparation of catalytic subunit E1 of pyruvate dehydrogenase complex, without cofactors thiamine diphosphate and Mg2+, no evidence of disorder/order loop transformations. Comparison with holo-E1 enzyme and in an inhibitor complex with thiamine 2-thiazolone diphosphate Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
thiamine 2-thiazolone diphosphate crystallization data of complex with enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AFG8
-
-

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
Escherichia coli