Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Reaction: 3.6.1.19/3.6.1.23

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

EC Number: 3.6.1.19 , 3.6.1.23

Enzymes and Genes:
pyrimidine deoxynucleoside triphosphate pyrophosphohydrolase Inferred from experiment : nudI
deoxyuridine triphosphatase Inferred from experiment : dut
nucleoside triphosphate pyrophosphohydrolase : mazG

In Pathway: superpathway of pyrimidine deoxyribonucleotides de novo biosynthesis (E. coli) , pyrimidine deoxyribonucleotides de novo biosynthesis I , pyrimidine deoxyribonucleotides dephosphorylation , pyrimidine deoxyribonucleotides de novo biosynthesis II

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 for 3.6.1.19: nucleoside-triphosphate diphosphatase

Enzyme Commission Synonyms for 3.6.1.19: nucleoside-triphosphate pyrophosphatase

Enzyme Commission Primary Name for 3.6.1.23: dUTP diphosphatase

Enzyme Commission Synonyms for 3.6.1.23: deoxyuridine-triphosphatase, dUTPase, dUTP pyrophosphatase, desoxyuridine 5'-triphosphate nucleotidohydrolase, desoxyuridine 5'-triphosphatase

Summary:
This reaction is part of pyrimidine nucleotide metabolism.

Enzyme Commission Summary for 3.6.1.19:
May be identical with EC 3.6.1.9 nucleotide diphosphatase.

Citations: [Chern69, Zhang02, BERTANI63, Giroir87, GREENBERG62, Grindey71]

Gene-Reaction Schematic: ?

Instance reactions of [a nucleoside triphosphate + H2O → a nucleoside 5'-monophosphate + diphosphate + H+] (3.6.1.19):
i1: CTP + H2O → CMP + diphosphate + H+ (3.6.1.65)

i2: dATP + H2O → dAMP + diphosphate + H+ (3.6.1.19)

i3: dUTP + H2O → dUMP + diphosphate + H+ (3.6.1.19/3.6.1.23)
i4: dGTP + H2O → dGMP + diphosphate + H+ (3.6.1.19)

i5: dITP + H2O → dIMP + diphosphate + H+ (3.6.1.66)

i6: ITP + H2O → IMP + diphosphate + H+ (3.6.1.19)

i7: XTP + H2O → XMP + diphosphate + H+ (3.6.1.66)

i8: ATP + H2O → AMP + diphosphate + H+ (3.6.1.8)

i9: dTTP + H2O → dTMP + diphosphate + H+ (3.6.1.19)

i10: UTP + H2O → UMP + diphosphate + H+ (3.6.1.19)

i11: dCTP + H2O → dCMP + diphosphate + H+ (3.6.1.12/3.6.1.19/3.6.1.65)

Relationship Links: BRENDA:EC:3.6.1.19 , BRENDA:EC:3.6.1.23 , ENZYME:EC:3.6.1.19 , ENZYME:EC:3.6.1.23 , IUBMB-ExplorEnz:EC:3.6.1.19 , IUBMB-ExplorEnz:EC:3.6.1.23


References

BERTANI63: BERTANI LE, HAEGGMARK A, REICHARD P (1963). "ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. II. FORMATION AND INTERCONVERSION OF DEOXYURIDINE PHOSPHATES." J Biol Chem 238;3407-13. PMID: 14085395

Chern69: Chern CJ, MacDonald AB, Morris AJ (1969). "Purification and properties of a nucleoside triphosphate pyrophosphohydrolase from red cells of the rabbit." J Biol Chem 244(20);5489-95. PMID: 4310599

Giroir87: Giroir LE, Deutsch WA (1987). "Drosophila deoxyuridine triphosphatase. Purification and characterization." J Biol Chem 262(1);130-4. PMID: 3025197

GREENBERG62: GREENBERG GR, SOMERVILLE RL (1962). "Deoxyuridylate kinase activity and deoxyuridinetriphosphatase in Escherichia coli." Proc Natl Acad Sci U S A 48;247-57. PMID: 13901467

Grindey71: Grindey GR, Nichol CA (1971). "Mammalian deoxyuridine 5'-triphosphate pyrophosphatase." Biochim Biophys Acta 240(2);180-3. PMID: 5105331

Zhang02: Zhang J, Inouye M (2002). "MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with Era, an essential GTPase in Escherichia coli." J Bacteriol 184(19);5323-9. PMID: 12218018


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 Thu Nov 27, 2014, biocyc13.