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Escherichia coli K-12 substr. MG1655 Reaction: 3.6.1.65

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

EC Number: 3.6.1.65

Enzymes and Genes:
nucleoside triphosphate pyrophosphohydrolase : mazG

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: (d)CTP diphosphatase

Enzyme Commission Synonyms: (d)CTP pyrophosphohydrolase, (d)CTP diphosphohydrolase, nudG (gene name)

Enzyme Commission Summary:
The enzyme, characterized from the bacterium Escherichia coli, is specific for the pyrimidine nucleotides CTP and dCTP. It also acts on 5-methyl-dCTP, 5-hydroxy-CTP and 8-hydroxy-dGTP.

Citations: [OHandley01, Fujikawa02, Iida05]

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:3.6.1.65 , ENZYME:EC:3.6.1.65 , IUBMB-ExplorEnz:EC:3.6.1.65


References

Fujikawa02: Fujikawa K, Kasai H (2002). "The oxidized pyrimidine ribonucleotide, 5-hydroxy-CTP, is hydrolyzed efficiently by the Escherichia coli recombinant Orf135 protein." DNA Repair (Amst) 1(7);571-6. PMID: 12509230

Iida05: Iida E, Satou K, Mishima M, Kojima C, Harashima H, Kamiya H (2005). "Amino acid residues involved in substrate recognition of the Escherichia coli Orf135 protein." Biochemistry 44(15);5683-9. PMID: 15823026

OHandley01: O'Handley SF, Dunn CA, Bessman MJ (2001). "Orf135 from Escherichia coli Is a Nudix hydrolase specific for CTP, dCTP, and 5-methyl-dCTP." J Biol Chem 2001;276(8);5421-6. PMID: 11053429


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 Fri Nov 28, 2014, biocyc13.