dCTP deaminase
In enzymology, a dCTP deaminase (EC 3.5.4.13) is an enzyme that catalyzes the chemical reaction
- dCTP + H2O dUTP + NH3
| dCTP deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.4.13 | ||||||||
| CAS number | 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 | ||||||||
| |||||||||
Thus, 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.
gollark: No, Turing completeness means it can simulate any Turing machine. It *can't* do that if it has limited memory.
gollark: I don't know exactly what its instruction set is like. But if it has finite-sized addresses, it can probably access finite amounts of memory, and thus is not Turing-complete.
gollark: *Languages* can be, since they often don't actually specify memory limits, implementations do.
gollark: It's not Turing-complete if it has limited memory.
gollark: Not *really*. In languages with an abstract model that doesn't specify limited memory sizes, yes, but PotatOS Assembly Language™'s addresses are 16 bits, so you can't address any more RAM than that.
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.
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