Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.4.1 extracted from

  • Seifert, F.; Golbik, R.; Brauer, J.; Lilie, H.; Schroeder-Tittmann, K.; Hinze, E.; Korotchkina, L.G.; Patel, M.S.; Tittmann, K.
    Direct kinetic evidence for half-of-the-sites reactivity in the E1 component of the human pyruvate dehydrogenase multienzyme complex through alternating sites cofactor activation (2006), Biochemistry, 45, 12775-12785.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
methyl acetylphosphonate phosphonate analogue of pyruvate, leading to formation of a stable 1’,4’-imino-2-alpha-phosphonolactyl-thiamindiphosphate Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information detailed kinetic and thermodynamic analysis Homo sapiens
0.01
-
pyruvate pH 7.6, 30°C, presence of 0.3 M KCl Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 active center communication between the cofactors in the enzyme complex. Only one of the thiamine molecules bound to the two active sites is in a chemically activated state whereas the thiamin in the inactive states ionizes with a rate that is at least three orders of magnitude smaller. Model of an active site synchronization via a proton wire that keeps the two active sites in an alternating activation state Homo sapiens

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.077
-
pyruvate pH 7.6, 30°C, presence of 0.3 M KCl Homo sapiens

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate KD value 0.00047 mM Homo sapiens