|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
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 for 18.104.22.168: dCTP diphosphatase
Enzyme Commission Synonyms for 22.214.171.124: deoxycytidine-triphosphatase, dCTP pyrophosphatase, deoxycytidine triphosphatase, deoxy-CTPase, dCTPase
Enzyme Commission Primary Name for 126.96.36.199: nucleoside-triphosphate diphosphatase
Enzyme Commission Synonyms for 188.8.131.52: nucleoside-triphosphate pyrophosphatase
Enzyme Commission Primary Name for 184.108.40.206: (d)CTP diphosphatase
Enzyme Commission Synonyms for 220.127.116.11: (d)CTP pyrophosphohydrolase, (d)CTP diphosphohydrolase, nudG (gene name)
Enzyme Commission Summary for 18.104.22.168:
Also hydrolyses dCDP to dCMP and phosphate.
Enzyme Commission Summary for 22.214.171.124:
May be identical with EC 126.96.36.199 nucleotide diphosphatase.
Enzyme Commission Summary for 188.8.131.52:
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.
Relationship Links: BRENDA:EC:184.108.40.206, BRENDA:EC:220.127.116.11, BRENDA:EC:18.104.22.168, ENZYME:EC:22.214.171.124, ENZYME:EC:126.96.36.199, ENZYME:EC:188.8.131.52, IUBMB-ExplorEnz:EC:184.108.40.206, IUBMB-ExplorEnz:EC:220.127.116.11, IUBMB-ExplorEnz:EC:18.104.22.168
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
Fujikawa02a: 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
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