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Literature summary for 2.1.1.45 extracted from

  • Dasgupta, T.; Anderson, K.S.
    Probing the role of parasite-specific, distant structural regions on communication and catalysis in the bifunctional thymidylate synthase-dihydrofolate reductase from Plasmodium falciparum (2008), Biochemistry, 47, 1336-1345.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum P13922
-
-
Plasmodium falciparum TM4/8.2 P13922
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + dUMP
-
Plasmodium falciparum dihydrofolate + dTMP
-
?
5,10-methylenetetrahydrofolate + dUMP
-
Plasmodium falciparum TM4/8.2 dihydrofolate + dTMP
-
?

Synonyms

Synonyms Comment Organism
thymidylate synthase-dihydrofolate reductase bifunctional enzyme Plasmodium falciparum
TS-DHFR
-
Plasmodium falciparum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.84
-
5,10-methylenetetrahydrofolate D4 N-terminal tail mutant enzyme Plasmodium falciparum
1.2
-
5,10-methylenetetrahydrofolate wild type enzyme Plasmodium falciparum
1.4
-
5,10-methylenetetrahydrofolate Ala-FACE mutant enzyme with residues 284, 285, 288, 289, and 292 mutated to Ala Plasmodium falciparum

Cofactor

Cofactor Comment Organism Structure
N5,N10-methylenetetrahydrofolate
-
Plasmodium falciparum