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Literature summary for 2.1.1.45 extracted from

  • Anderson, A.C.; O'Neil, R.H.; DeLano, W.L.; Stroud, R.M.
    The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits (1999), Biochemistry, 38, 13829-13836.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals belong to space group P2(1)2(1)2(1), a = 54.05 A, b = 66.16 A and c = 178.76 A Pneumocystis carinii

Inhibitors

Inhibitors Comment Organism Structure
CB3717
-
Pneumocystis carinii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5,10-methylenetetrahydrofolate + dUMP Pneumocystis carinii biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism dihydrofolate + dTMP
-
?

Organism

Organism UniProt Comment Textmining
Pneumocystis carinii P13100
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pneumocystis carinii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + dUMP
-
Pneumocystis carinii dihydrofolate + dTMP
-
r
5,10-methylenetetrahydrofolate + dUMP biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism Pneumocystis carinii dihydrofolate + dTMP
-
?

Subunits

Subunits Comment Organism
dimer
-
Pneumocystis carinii

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00009
-
CB3717
-
Pneumocystis carinii