Crystallization (Comment) | Organism |
---|---|
mutants S88A and S88C, to 1.95 and 2.05 A resolution, respectively. Structure reveals minimlas changes in folding and active site conformation compared to wild-type. There is no covalent bond between the cysteine and dUMP in the crystal | Thermotoga maritima |
Protein Variants | Comment | Organism |
---|---|---|
S88A | mutant retains activity. Residue S88 is not required for catalysis | Thermotoga maritima |
S88C | mutant retains activity. Residue S88 is not required for catalysis | Thermotoga maritima |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermotoga maritima | Q9WYT0 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
5,10-methylenetetrahydrofolate + dUMP + NADPH + H+ = dTMP + tetrahydrofolate + NADP+ | a hydride equivalent is transferred from the reduced flavin cofactor directly to the uracil ring, followed by an isomerization of the intermediate to form the product, 2'-deoxythymidine-5'-monophosphate | Thermotoga maritima |