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Literature summary extracted from

  • Groff, D.; Thielges, M.C.; Cellitti, S.; Schultz, P.G.; Romesberg, F.E.
    Efforts toward the direct experimental characterization of enzyme microenvironments: tyrosine100 in dihydrofolate reductase (2009), Angew. Chem. Int. Ed. Engl., 48, 3478-3481.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.3 expression in Escherichia coli Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.3 additional information
-
 additional information molecular dynamics and spectroscopic analysis of the enzyme in transition state based on residues Tyr100 and Tyr111, overview 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 P0ABQ4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.3 recombinant enzyme from Escherichia coli 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+
-
 ?
1.5.1.3 7,8-dihydrofolate + NADPH + H+ DHFR catalyzes hydride transfer from the cofactor NADPH to 7,8-dihydrofolate to produce tetrahydrofolate requiring electrostatic complementarity between the enzyme and the transition state 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