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

BRENDA support

Literature summary for 1.5.1.3 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
Search for more literature for 1.5.1.3

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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)

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 P0ABQ4
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli 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+
-
 ?
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

Synonyms Comment Organism
DHFR
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Escherichia coli