Sepiapterin deaminase
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 | This article includes a list of references, related reading, or external links, but its sources remain unclear because it lacks inline citations. (October 2019) |
| sepiapterin deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.4.24 | ||||||||
| CAS no. | 62213-22-3 | ||||||||
| 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 sepiapterin deaminase (EC 3.5.4.24) is an enzyme that catalyzes the chemical reaction
- sepiapterin + H2O xanthopterin-B2 + NH3
Thus, the two substrates of this enzyme are sepiapterin and H2O whereas its two products are xanthopterin-B2 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 sepiapterin aminohydrolase.
References[edit]
- Tsusué M (April 1971). "Studies on sepiapterin deaminase from the silkworm, Bombyx mori. Purification and some properties of the enzyme". Journal of Biochemistry. 69 (4): 781–8. PMID 5572808.
