The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: peptidylglycine monooxygenase
Reaction: peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
Other name(s): peptidylglycine 2-hydroxylase; peptidyl α-amidating enzyme; peptide-α-amide synthetase; synthase, peptide α-amide; peptide α-amidating enzyme; peptide α-amide synthase; peptidylglycine α-hydroxylase; peptidylglycine α-amidating monooxygenase; PAM-A; PAM-B; PAM
Systematic name: peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating)
Comments: A copper protein. Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme. The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalysed by EC peptidylamidoglycolate lyase. Involved in the final step of biosynthesis of α-melanotropin and related biologically active peptides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 90597-47-0
1.  Bradbury, A.F., Finnie, M.D.A. and Smyth, D.G. Mechanism of C-terminal amide formation by pituitary enzymes. Nature (Lond.) 298 (1982) 686–688. [PMID: 7099265]
2.  Bradbury, A.F. and Smyth, D.G. Enzyme-catalysed peptide amidation. Isolation of a stable intermediate formed by reaction of the amidating enzyme with an imino acid. Eur. J. Biochem. 169 (1987) 579–584. [PMID: 3691506]
3.  Glembotski, C.G. Further characterization of the peptidyl α-amidating enzyme in rat anterior pituitary secretory granules. Arch. Biochem. Biophys. 241 (1985) 673–683. [PMID: 2994573]
4.  Katopodis, A.G., Ping, D. and May, S.W. A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of α-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine α-amidating monooxygenase in peptide amidation. Biochemistry 29 (1990) 6115–6120. [PMID: 2207061]
5.  Murthy, A.S.N., Keutmann, H.T. and Eipper, B.A. Further characterization of peptidylglycine α-amidating monooxygenase from bovine neurointermediate pituitary. Mol. Endocrinol. 1 (1987) 290–299. [PMID: 3453894]
6.  Murthy, A.S.N., Mains, R.E. and Eipper, B.A. Purification and characterization of peptidylglycine α-amidating monooxygenase from bovine neurointermediate pituitary. J. Biol. Chem. 261 (1986) 1815–1822. [PMID: 3944110]
[EC created 1989]

Data © 2001–2016 IUBMB
Web site © 2005–2016 Andrew McDonald