| pterin deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.4.11 | ||||||||
| CAS no. | 9025-04-1 | ||||||||
| 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 | ||||||||
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In enzymology, a pterin deaminase (EC 3.5.4.11) is an enzyme that catalyzes the chemical reaction
- 2-amino-4-hydroxypteridine + H2O 2,4-dihydroxypteridine + NH3
2,4-dihydroxypteridine + NH3Thus, the two substrates of this enzyme are 2-amino-4-hydroxypteridine and H2O, whereas its two products are 2,4-dihydroxypteridine 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 2-amino-4-hydroxypteridine aminohydrolase. This enzyme is also called acrasinase.
References
- LEVENBERG B, HAYAISHI O (1959). "A bacterial pterin deaminase". J. Biol. Chem. 234 (4): 955–61. PMID 13654299.
- Rembold H, Simmersbach F (1969). "Catabolism of pteridine cofactors. II. A specific pterin deaminase in rat liver". Biochim. Biophys. Acta. 184 (3): 589–96. doi:10.1016/0304-4165(69)90273-6. PMID 5821022.
| 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 | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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