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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate + CoA + NAD+ | - |
Homo sapiens | acetyl-CoA + CO2 + NADH | - |
? |
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 | Comment | Organism | Structure |
---|---|---|---|
thiamine diphosphate | KD value 0.00047 mM | Homo sapiens |