Biology:Peptidylglycine monooxygenase
| peptidylglycine monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.17.3 | ||||||||
| CAS number | 90597-47-0 | ||||||||
| 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 peptidylglycine monooxygenase (EC 1.14.17.3) is an enzyme that catalyzes the chemical reaction
- peptidylglycine + ascorbate + O2 [math]\displaystyle{ \rightleftharpoons }[/math] peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
The 3 substrates of this enzyme are peptidylglycine, ascorbate, and O2, whereas its 3 products are peptidyl(2-hydroxyglycine), dehydroascorbate, and H2O.
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 reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating). Other names in common use include 2-hydroxylase, alpha-amidating enzyme, peptide-alpha-amide synthetase, synthase, peptide alpha-amide, peptide alpha-amidating enzyme, peptide alpha-amide synthase, alpha-hydroxylase, alpha-amidating monooxygenase, PAM-A, PAM-B, and PAM. It employs one cofactor, copper.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1OPM, 1PHM, 1SDW, 1YI9, 1YIP, 1YJK, 1YJL, and 3PHM.
References
- "Mechanism of C-terminal amide formation by pituitary enzymes". Nature 298 (5875): 686–8. 1982. doi:10.1038/298686a0. PMID 7099265. Bibcode: 1982Natur.298..686B.
- "Enzyme-catalysed peptide amidation. Isolation of a stable intermediate formed by reaction of the amidating enzyme with an imino acid". Eur. J. Biochem. 169 (3): 579–84. 1987. doi:10.1111/j.1432-1033.1987.tb13648.x. PMID 3691506.
- Glembotski CC (1985). "Further characterization of the peptidyl alpha-amidating enzyme in rat anterior pituitary secretory granules". Arch. Biochem. Biophys. 241 (2): 673–83. doi:10.1016/0003-9861(85)90594-6. PMID 2994573.
- "A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of alpha-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine alpha-amidating monooxygenase in peptide amidation". Biochemistry 29 (26): 6115–20. 1990. doi:10.1021/bi00478a001. PMID 2207061.
- "Further characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary". Mol. Endocrinol. 1 (4): 290–9. 1987. doi:10.1210/mend-1-4-290. PMID 3453894.
- "Purification and characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary". J. Biol. Chem. 261 (4): 1815–22. 1986. PMID 3944110.
 |  |
