EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.27 | Sus scrofa | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.1.1.27 | heart | - |
Sus scrofa | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.27 | oxamate + NADH | two distinct active site LDH/NADH-oxamate complex conformations, a major populated structure wherein all significant hydrogen-bonding patterns are formed at the active site between protein and bound ligand necessary for the catalytically productive Michaelis complex and, a minor structure in a configuration of the active site that is unfavorable to carry out catalyzed chemistry. This latter structure likely simulates a dead-end complex in the reaction mixture. The evolution of the encounter complex between LDH/NADH and oxamate collapses via a branched reaction pathway to form the major and minor bound species. Once the encounter complex is formed between LDH/NADH and substrate, the ternary protein-ligand complex appears to fold to form a compact productive complex in an all or nothing like fashion with all the important molecular interactions coming together at the same time | Sus scrofa | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.27 | lactate dehydrogenase | - |
Sus scrofa |
1.1.1.27 | LDH | - |
Sus scrofa |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.27 | NADH | - |
Sus scrofa |