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 studiesedit
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.
Referencesedit
Bradbury AF, Finnie MD, Smyth DG (1982). "Mechanism of C-terminal amide formation by pituitary enzymes". Nature. 298 (5875): 686–8. Bibcode:1982Natur.298..686B. doi:10.1038/298686a0. PMID 7099265. S2CID 4324776.
Bradbury AF, Smyth DG (1987). "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. 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.
Katopodis AG, Ping D, May SW (1990). "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. doi:10.1021/bi00478a001. PMID 2207061.
Murthy AS, Keutmann HT, Eipper BA (1987). "Further characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary". Mol. Endocrinol. 1 (4): 290–9. doi:10.1210/mend-1-4-290. PMID 3453894.
Murthy AS, Mains RE, Eipper BA (1986). "Purification and characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary". J. Biol. Chem. 261 (4): 1815–22. PMID 3944110.
peptidylglycine, monooxygenase, enzymology, peptidylglycine, monooxygenase, enzyme, that, catalyzes, chemical, reactionpeptidylglycine, monooxygenaseidentifiersec, 3cas, 90597, 0databasesintenzintenz, viewbrendabrenda, entryexpasynicezyme, viewkeggkegg, entrym. In enzymology a peptidylglycine monooxygenase EC 1 14 17 3 is an enzyme that catalyzes the chemical reactionpeptidylglycine monooxygenaseIdentifiersEC no 1 14 17 3CAS no 90597 47 0DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteins peptidylglycine ascorbate O2 displaystyle rightleftharpoons 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 editAs 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 editBradbury AF Finnie MD Smyth DG 1982 Mechanism of C terminal amide formation by pituitary enzymes Nature 298 5875 686 8 Bibcode 1982Natur 298 686B doi 10 1038 298686a0 PMID 7099265 S2CID 4324776 Bradbury AF Smyth DG 1987 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 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 Katopodis AG Ping D May SW 1990 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 doi 10 1021 bi00478a001 PMID 2207061 Murthy AS Keutmann HT Eipper BA 1987 Further characterization of peptidylglycine alpha amidating monooxygenase from bovine neurointermediate pituitary Mol Endocrinol 1 4 290 9 doi 10 1210 mend 1 4 290 PMID 3453894 Murthy AS Mains RE Eipper BA 1986 Purification and characterization of peptidylglycine alpha amidating monooxygenase from bovine neurointermediate pituitary J Biol Chem 261 4 1815 22 PMID 3944110 Portal nbsp Biology This EC 1 14 enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Peptidylglycine monooxygenase amp oldid 1172356555, wikipedia, wiki, book, books, library,
