Peptide-aspartate beta-dioxygenase
| peptide-aspartate beta-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.11.16 | ||||||||
| CAS no. | 122544-66-5 | ||||||||
| 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 peptide-aspartate beta-dioxygenase (EC 1.14.11.16), a member of the alpha-ketoglutarate-dependent hydroxylases superfamily, is an enzyme that catalyzes the chemical reaction
- peptide-L-aspartate + 2-oxoglutarate + O2 peptide-3-hydroxy-L-aspartate + succinate + CO2
The 3 substrates of this enzyme are peptide-L-aspartate, 2-oxoglutarate, and O2, whereas its 3 products are peptide-3-hydroxy-L-aspartate, succinate, and CO2.
It employs one cofactor, iron.
Nomenclature
[edit]This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is peptide-L-aspartate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include aspartate beta-hydroxylase, and aspartylpeptide beta-dioxygenase.
References
[edit]Further reading section
[edit]- Gronke RS, Welsch DJ, VanDusen WJ, Garsky VM, Sardana MK, Stern AM, Friedman PA (May 1990). "Partial purification and characterization of bovine liver aspartyl beta-hydroxylase". The Journal of Biological Chemistry. 265 (15): 8558–65. doi:10.1016/S0021-9258(19)38924-0. PMID 2187868.
