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Literature summary extracted from

  • Maley, F.; Pedersen-Lane, J.; Changchien, L.
    Complete restoration of activity to inactive mutants of Escherichia coli thymidylate synthase: Evidence that E. coli thymidylate synthase is a half-the-sites activity enzyme (1995), Biochemistry, 34, 1469-1474.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.45
-
 Escherichia coli
2.1.1.45
-
 Lacticaseibacillus casei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.45 5,10-methylenetetrahydrofolate + dUMP Escherichia coli
-
 dihydrofolate + dTMP
-
 ?
2.1.1.45 5,10-methylenetetrahydrofolate + dUMP Lacticaseibacillus casei
-
 dihydrofolate + dTMP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.45 Escherichia coli
-
-
-
2.1.1.45 Lacticaseibacillus casei
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.45 5,10-methylenetetrahydrofolate + dUMP
-
 Escherichia coli dihydrofolate + dTMP
-
 ?
2.1.1.45 5,10-methylenetetrahydrofolate + dUMP
-
 Escherichia coli dihydrofolate + dTMP
-
 r
2.1.1.45 5,10-methylenetetrahydrofolate + dUMP
-
 Lacticaseibacillus casei dihydrofolate + dTMP
-
 ?
2.1.1.45 5,10-methylenetetrahydrofolate + dUMP
-
 Lacticaseibacillus casei dihydrofolate + dTMP
-
 r

Subunits

EC Number Subunits Comment Organism
2.1.1.45 dimer
-
 Escherichia coli
2.1.1.45 dimer
-
 Lacticaseibacillus casei