|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
Enzymes and Genes:
|Escherichia coli K-12 substr. MG1655 :||dihydrofolate reductase
dihydrofolate reductase : folA
|Glycine max :||dihydrofolate reductase
|Homo sapiens :||dihydrofolate reductase-like protein 1
|Pisum sativum :||dihydrofolate reductase/thymidylate synthase
|Thermotoga maritima :||dihydrofolate reductase
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: dihydrofolate reductase
Enzyme Commission Synonyms: tetrahydrofolate dehydrogenase, DHFR, pteridine reductase:dihydrofolate reductase, dihydrofolate reductase:thymidylate synthase, thymidylate synthetase-dihydrofolate reductase, folic acid reductase, folic reductase, dihydrofolic acid reductase, dihydrofolic reductase, 7,8-dihydrofolate reductase, NADPH-dihydrofolate reductase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 5.5057983 [Latendresse13]
Enzyme Commission Summary:
Tetrahydrofolate is a C1 donor involved in many metabolic processes. It is an essential step for de novo glycine and purine synthesis, DNA precursor synthesis and for conversion of dUMP to dTMP.
Bolin82: Bolin JT, Filman DJ, Matthews DA, Hamlin RC, Kraut J (1982). "Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate." J Biol Chem 257(22);13650-62. PMID: 6815178
Young69: Young IG, Gibson F (1969). "Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli." Biochim Biophys Acta 177(3);401-11. PMID: 4306838
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