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Literature summary extracted from

  • Oyeyemi, O.A.; Sours, K.M.; Lee, T.; Resing, K.A.; Ahn, N.G.; Klinman, J.P.
    Temperature dependence of protein motions in a thermophilic dihydrofolate reductase and its relationship to catalytic efficiency (2010), Proc. Natl. Acad. Sci. USA, 107, 10074-10079.
    View publication on PubMedView publication on EuropePMC

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+ Geobacillus stearothermophilus
-
 5,6,7,8-tetrahydrofolate + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.3 Geobacillus stearothermophilus
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.5.1.3 5,6,7,8-tetrahydrofolate: NADP+ oxidoreductase
-
 Geobacillus stearothermophilus
1.5.1.3 DHFR
-
 Geobacillus stearothermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.5.1.3 67
-
 the melting temperature is 67°C Geobacillus stearothermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.3 NADPH
-
 Geobacillus stearothermophilus