Crystallization (Comment) | Organism |
---|---|
purified enzyme E1 in complex with inhibitor thiamine thiazolone diphosphate and Mg2+, sitting drop vapour diffusion method, reservoir solution: 15-20% PEG 2000 monomethyl ether, 5-10% 2-propanol, 0.2% NaN3, 100 mM HEPES, pH 7.00, 22°C, 4 weeks, X-ray diffraction structure determination and analysis at 2.09 A resolution, comparison with structure determined with bound cofactor thiamine diphosphate | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
thiamine thiazolone diphosphate | inhibits potently the E1 component of the pyruvate dehydrogenase multienzyme complex PDHc, competitive to cofactor thiamine diphosphate, binding structure and determinants, binding induced reorganisation of the active site conformation, mechanism, K392 is important, overview | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate + CoA + NAD+ | Escherichia coli | enzyme E1 is a component of the pyruvate dehydrogenase multienzyme complex PDHc, and catalyzes the first step of the multistep process | acetyl-CoA + CO2 + NADH | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0AFG8 | enzyme E1 is a component of the pyruvate dehydrogenase multienzyme complex PDHc | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 | reaction mechanism, role of water molecules | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate + CoA + NAD+ | - |
Escherichia coli | acetyl-CoA + CO2 + NADH | - |
? | |
pyruvate + CoA + NAD+ | enzyme E1 is a component of the pyruvate dehydrogenase multienzyme complex PDHc, and catalyzes the first step of the multistep process | Escherichia coli | acetyl-CoA + CO2 + NADH | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PDHc E1 | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Escherichia coli | |
thiamine diphosphate | dependent on, binding structure and determinants, V conformation, K392 is important | Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.003 | - |
thiamine thiazolone diphosphate | - |
Escherichia coli |