Peptide-aspartate beta-dioxygenase
| peptide-aspartate beta-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.11.16 | ||||||||
| CAS number | 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 / EGO | ||||||||
| |||||||||
In enzymology, a peptide-aspartate beta-dioxygenase (EC 1.14.11.16) 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.
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. It employs one cofactor, iron.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1YCI, 2CGN, 2CGO, and 2ILM.
References
- Friedman PA; Welsch, DJ; Vandusen, WJ; Garsky, VM; Sardana, MK; Stern, AM; Friedman, PA (1990). "Partial purification and characterization of bovine liver aspartyl beta-hydroxylase". J. Biol. Chem. 265 (15): 8558–65. PMID 2187868.