Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.148 extracted from

  • Agrawal, N.; Lesley, S.A.; Kuhn, P.; Kohen, A.
    Mechanistic studies of a flavin-dependent thymidylate synthase (2004), Biochemistry, 43, 10295-10301.
    View publication on PubMed

Application

Application Comment Organism
medicine the unique mechanism of FDTS makes it an attractive target for antibiotic drug development Thermotoga maritima

Inhibitors

Inhibitors Comment Organism Structure
NADPH
-
Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Thermotoga maritima the enzyme is essential to DNA replication ?
-
?
additional information Thermotoga maritima DSM 3109 the enzyme is essential to DNA replication ?
-
?

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9WYT0 TM0449
-
Thermotoga maritima DSM 3109 Q9WYT0 TM0449
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is essential to DNA replication Thermotoga maritima ?
-
?
additional information the enzyme is essential to DNA replication Thermotoga maritima DSM 3109 ?
-
?

Synonyms

Synonyms Comment Organism
FDTS
-
Thermotoga maritima
flavin-dependent TS
-
Thermotoga maritima

Cofactor

Cofactor Comment Organism Structure
FAD the pro-R hydride of NADPH and not the R6 hydride of the tetrahydropterin is the reducing agent. The stereospecificity for the pro-R NADPH oxidation is not absolute. The hydride is transferred to FAD, which is the rate-limiting step of the catalytic cascade Thermotoga maritima
NADPH the pro-R hydride of NADPH and not the R6 hydride of the tetrahydropterin is the reducing agent. The stereospecificity for the pro-R NADPH oxidation is not absolute. The hydride is transferred to FAD, which is the rate-limiting step of the catalytic cascade Thermotoga maritima