| dCTP deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.4.13 | ||||||||
| CAS no. | 37289-18-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a dCTP deaminase (EC 3.5.4.13) is an enzyme that catalyzes the chemical reaction
- dCTP + H2O dUTP + NH3
dUTP + NH3Thus, the two substrates of this enzyme are dCTP and H2O, whereas its two products are dUTP and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is dCTP aminohydrolase. Other names in common use include deoxycytidine triphosphate deaminase, and 5-methyl-dCTP deaminase. This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1OGH, 1PKH, 1PKJ, 1PKK, 1XS1, 1XS4, 1XS6, 2J4H, and 2J4Q.
References
- Tomita F, Takahashi I (1969). "A novel enzyme, dCTP deaminase, found in Bacillus subtilis infected with phage PBS I". Biochim. Biophys. Acta. 179 (1): 18–27. doi:10.1016/0005-2787(69)90117-8. PMID 4976547.
| Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
|---|---|
| 3.5.1: Linear amides / Amidohydrolases | |
| 3.5.2: Cyclic amides/ Amidohydrolases | |
| 3.5.3: Linear amidines/ Ureohydrolases | |
| 3.5.4: Cyclic amidines/ Aminohydrolases | |
| 3.5.5: Nitriles/ Aminohydrolases | |
| 3.5.99: Other | |
| Enzymes | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
|
This EC 3.5 enzyme-related article is a stub. You can help Misplaced Pages by expanding it. |