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Literature summary for 1.2.4.1 extracted from

  • Seifert, F.; Ciszak, E.; Korotchkina, L.; Golbik, R.; Spinka, M.; Dominiak, P.; Sidhu, S.; Brauer, J.; Patel, M.S.; Tittmann, K.
    Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex (2007), Biochemistry, 46, 6277-6287.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli M15 cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
vapour diffusion method with 14-18% PEG 3350, 0.1 mM sodium azide, and 200 mM NaSCN in 50 mM potassium phosphate (pH 8.0) Homo sapiens

Protein Variants

Protein Variants Comment Organism
S264E pseudophosphorylation mutant, the preceding binding of substrate to the enzyme's active site via the substrate channel and the subsequent reductive acetylation of the E2 component are severely slowed in the mutant enzyme Homo sapiens
S264Q selectively deficient in pyruvate binding and reductive acetylation of component E2 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P08559
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphorylation phosphorylation of Ser264 slows the preceding binding of substrate to the enzyme's active site via the substrate channel and the subsequent reductive acetylation of the E2 component Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + CoA + NAD+
-
Homo sapiens acetyl-CoA + CO2 + NADH
-
ir

Synonyms

Synonyms Comment Organism
PDHc-E1
-
Homo sapiens
thiamin-dependent pyruvate dehydrogenase part of the pyruvate dehydrogenase multienzyme complex PDHc as component E1 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens
thiamine diphosphate dependent Homo sapiens