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Literature summary for 1.5.1.3 extracted from

  • Liu, C.T.; Wang, L.; Goodey, N.M.; Hanoian, P.; Benkovic, S.J.
    Temporally overlapped but uncoupled motions in dihydrofolate reductase catalysis (2013), Biochemistry, 52, 5332-5334.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
G121V the mutation reduces the hydride transfer efficiency by about 100fold Escherichia coli
L54I the mutation reduces the hydride transfer efficiency by about 100fold Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7,8-dihydrofolate + NADPH + H+ Escherichia coli
-
5,6,7,8-tetrahydrofolate + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydrofolate + NADPH + H+
-
Escherichia coli 5,6,7,8-tetrahydrofolate + NADP+
-
?

Synonyms

Synonyms Comment Organism
DHFR
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Escherichia coli