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MetaCyc Reaction: 1.5.1.3

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 1.5.1.3

Enzymes and Genes:

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

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

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. 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): 5.5057983Inferred 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

Unification Links: KEGG:R00939

Relationship Links: BRENDA:EC:1.5.1.3, ENZYME:EC:1.5.1.3, IUBMB-ExplorEnz:EC:1.5.1.3

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


References

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 Pathway Tools version 19.5 (software by SRI International) on Sun May 1, 2016, biocyc14.