Cysteamine dioxygenase
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| cysteamine dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.11.19 | ||||||||
| CAS no. | 9033-41-4 | ||||||||
| 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 cysteamine dioxygenase (EC 1.13.11.19) is an enzyme that catalyzes the chemical reaction
- 2-aminoethanethiol + O2 hypotaurine
Thus, the two substrates of this enzyme are 2-aminoethanethiol and O2, whereas its product is hypotaurine.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 2-aminoethanethiol:oxygen oxidoreductase. Other names in common use include persulfurase, cysteamine oxygenase, and cysteamine:oxygen oxidoreductase. This enzyme participates in taurine and hypotaurine metabolism. It employs one cofactor, iron.
References
- Cavallini D, De Marco C, Scandurra R, Dupre S, Graziani MT (1966). "The enzymatic oxidation of cysteamine to hypotaurine. Purification and properties of the enzyme". J. Biol. Chem. 241 (13): 3189–96. PMID 5912113.
- Wood JL, Cavallini D (1967). "Enzymic oxidation of cysteamine to hypotaurine in the absence of a cofactor". Arch. Biochem. Biophys. 119 (1): 368–72. doi:10.1016/0003-9861(67)90467-5. PMID 6052430.
- Cavallini D, Federici G, Ricci G, Dupre S, Antonucci A (1975). "The specificity of cysteamine oxygenase". FEBS Lett. 56 (2): 348–51. doi:10.1016/0014-5793(75)81124-0. PMID 1157952.
- Richerson RB, Ziegler DM (1987). "Sulfur and Sulfur Amino Acids. Cysteamine dioxygenase". Methods Enzymol. Methods in Enzymology. 143: 410–5. doi:10.1016/0076-6879(87)43071-1. ISBN 978-0-12-182043-5. PMID 3657558.
