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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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Escherichia coli K-12 substr. MG1655 Reaction: 1.3.1.1

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

EC Number: 1.3.1.1

Enzymes and Genes:
NAD-dependent dihydropyrimidine dehydrogenase Inferred from experiment Inferred by computational analysis : preT , preA

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: dihydropyrimidine dehydrogenase (NAD+)

Enzyme Commission Synonyms: dihydropyrimidine dehydrogenase, dihydrothymine dehydrogenase, pyrimidine reductase, thymine reductase, uracil reductase, dihydrouracil dehydrogenase (NAD+)

Enzyme Commission Summary:
An iron-sulfur flavoenzyme. The enzyme was originally discovered in the uracil-fermenting bacterium, Clostridium uracilicum, which utilizes uracil and thymine as nitrogen and carbon sources for growth [CAMPBELL57]. Since then the enzyme was found in additional organisms including Alcaligenes eutrophus [Schmitt96], Pseudomonas strains [Kim91, West01] and Escherichia coli [West98, Hidese11].

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.3.1.1 , ENZYME:EC:1.3.1.1 , IUBMB-ExplorEnz:EC:1.3.1.1


References

CAMPBELL57: CAMPBELL LL (1957). "Reductive degradation of pyrimidines. III. Purification and properties of dihydrouracil dehydrogenase." J Biol Chem 227(2);693-700. PMID: 13462991

Hidese11: Hidese R, Mihara H, Kurihara T, Esaki N (2011). "Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent heterotetramer essential for the production of 5,6-dihydrouracil." J Bacteriol 193(4);989-93. PMID: 21169495

Kim91: Kim S, West TP (1991). "Pyrimidine catabolism in Pseudomonas aeruginosa." FEMS Microbiol Lett 61(2-3);175-9. PMID: 1903745

Schmitt96: Schmitt U, Jahnke K, Rosenbaum K, Cook PF, Schnackerz KD (1996). "Purification and characterization of dihydropyrimidine dehydrogenase from Alcaligenes eutrophus." Arch Biochem Biophys 332(1);175-82. PMID: 8806723

West01: West TP (2001). "Pyrimidine base catabolism in Pseudomonas putida biotype B." Antonie Van Leeuwenhoek 80(2);163-7. PMID: 11759049

West98: West TP (1998). "Isolation and characterization of an Escherichia coli B mutant strain defective in uracil catabolism." Can J Microbiol 44(11);1106-9. PMID: 10030006


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, BIOCYC14B.