MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number:

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655 : dihydrofolate reductase Inferred from experiment : folM
dihydrofolate reductase Inferred from experiment : folA
Glycine max : dihydrofolate reductase Inferred from experiment : DHFR-TS
Homo sapiens : dihydrofolate reductase-like protein 1 Inferred from experiment : DHFRL1
Pisum sativum : dihydrofolate reductase/thymidylate synthase Inferred from experiment : dhfrts1
Thermotoga maritima : dihydrofolate reductase : dyrA

In Pathway: folate transformations II , tetrahydrofolate biosynthesis , N10-formyl-tetrahydrofolate biosynthesis

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 Inferred by computational analysis [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.

Citations: [Bolin82, Kaufman66, Young69]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC: , ENZYME:EC: , IUBMB-ExplorEnz:EC:

Created 11-Sep-2014 by Caspi R , SRI International


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

Kaufman66: Kaufman BT, Gardiner RC (1966). "Studies on dihydrofolic reductase. I. Purification and properties of dihydrofolic reductase from chicken liver." J Biol Chem 241(6);1319-28. PMID: 4379915

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Thu Oct 8, 2015, biocyc13.