Crystallization (Comment) | Organism |
---|---|
molecular dynamics simulations based on PDB entry 1K3T. The first stage of the reaction (oxidoreduction) takes place in the Pi site (energetically more favourable), with the formation of oxyanion thiohemiacetal and thioacylenzyme intermediates without acid-base assistance of His194. Residue Arg249 has an important role in the ability of the enzyme to bind the glyceraldehyde 3-phosphatesubstrate, which interacts with NAD+ and other important residues, such as Cys166, Glu109, Thr167, Ser247 and Thr226, in the GAPDH active site | Trypanosoma cruzi |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(3-[(4-nitrophenoxy)carbonyl]but-3-en-1-yl)phosphonic acid | - |
Trypanosoma cruzi | |
3-(p-nitrophenoxycarboxyl)-3-ethylene propyl dihydroxyphosphinate | propyl dihydroxyphosphonate analogue of substrate glyceraldehyde 3-phosphate. The energy profiles correspond to the nucleophilic attack of Cys166 on the atom C1 of the carbonyl group of the inhibitor. The barrier for the inhibition reaction is lower than that observed for a natural substrate | Trypanosoma cruzi |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Trypanosoma cruzi | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Trypanosoma cruzi | - |
- |
- |
Trypanosoma cruzi | P22513 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Trypanosoma cruzi | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GAPDH | - |
Trypanosoma cruzi |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Trypanosoma cruzi |