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Literature summary for 1.2.1.104 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
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 pyruvate E1 component, pH 7.6, 30°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P08559 and P11177 P08559 i.e. E1 component subunit alpha, P11177 i.e. E1 component subunit beta
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
60
-
 E1 component, pH 7.6, 30°C Homo sapiens

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
PdhA1
-
 Homo sapiens
PdhB1
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.077
-
 pyruvate E1 component, pH 7.6, 30°C Homo sapiens

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate only one of the two thiamine molecules bound to the two active sites of the alpha2beta2 E1 component is in a chemically activated state exhibiting an apparent C2 ionization rate constant of approximately 50 per s at pH 7.6 and 30°C, whereas the thiamine in the inactive site ionizes with a rate that is at least 3 orders of magnitude smaller Homo sapiens

General Information

General Information Comment Organism
physiological function the active centers of the alpha2beta2 E1 component are not equivalent. In the activated active site, pyruvate is rapidly bound and decarboxylated with apparent forward rate constants of covalent pyruvate binding of 2 per s and decarboxylation of the formed 2-lactylthiamine intermediate of 5 per s. In the dormant site, these steps are as slow as 0.03 per s Homo sapiens