Escherichia coli K-12 substr. MG1655 Reaction:

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

EC Number:

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

In Pathway: pyrimidine deoxyribonucleotides dephosphorylation

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: ?

Gene-Reaction Schematic

Instance reactions of [a nucleoside triphosphate + H2O → a nucleoside 5'-monophosphate + diphosphate + H+] (
i1: ATP + H2O → AMP + diphosphate + H+ (

i2: CTP + H2O → CMP + diphosphate + H+ (

i3: dCTP + H2O → dCMP + diphosphate + H+ (
i4: dUTP + H2O → dUMP + diphosphate + H+ (

i5: dTTP + H2O → dTMP + diphosphate + H+ (

i6: UTP + H2O → UMP + diphosphate + H+ (

i7: dATP + H2O → dAMP + diphosphate + H+ (

i8: dGTP + H2O → dGMP + diphosphate + H+ (

i9: dITP + H2O → dIMP + diphosphate + H+ (

i10: ITP + H2O → IMP + diphosphate + H+ (

i11: XTP + H2O → XMP + diphosphate + H+ (

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


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 19.0 on Fri Jul 31, 2015, biocyc12.