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Literature summary for 2.1.1.148 extracted from

  • Koehn, E.M.; Fleischmann, T.; Conrad, J.A.; Palfey, B.A.; Lesley, S.A.; Mathews, I.I.; Kohen, A.
    An unusual mechanism of thymidylate biosynthesis in organisms containing the thyX gene (2009), Nature, 458, 919-923.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

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

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

Organism UniProt Comment Textmining
Thermotoga maritima Q9WYT0
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Reaction

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