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Literature summary 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

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.3 7,8-dihydrofolate + NADPH + H+ Escherichia coli
-
5,6,7,8-tetrahydrofolate + NADP+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.3 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.3 7,8-dihydrofolate + NADPH + H+
-
Escherichia coli 5,6,7,8-tetrahydrofolate + NADP+
-
?

Synonyms

EC Number Synonyms Comment Organism
1.5.1.3 DHFR
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.3 NADPH
-
Escherichia coli