Пептидилглицин монооксигеназа
| Peptidilglicin monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.17.3 | ||||||||
| CAS broj | 90597-47-0 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Peptidilglicin monooksigenaza (EC 1.14.17.3, peptidilglicinska 2-hidroksilaza, peptidil alfa-amidirajući enzim, peptid-alfa-amidna sintetaza, sintaza, peptid alfa-amid, peptidni alfa-amidirajući enzim, peptidna alfa-amidna sintaza, peptidilglicinska alfa-hidroksilaza, peptidilglicinska alfa-amidirajuća monooksigenaza, PAM-A, PAM-B, PAM) je enzim sa sistematskim imenom peptidilglicin,askorbat:kiseonik oksidoreduktaza (2-hidroksilacija).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- peptidilglicin + askorbat + O2 peptidil(2-hidroksiglicin) + dehidroaskorbat + H2O
Ovaj enzim sadrži bakar. Peptidilglicini sa neutralnim aminokiselinskim ostatkom u pretposlednjoj poziciji su najbolji supstrati.
Reference
[уреди | уреди извор]- ^ Bradbury, A.F., Finnie, M.D.A. and Smyth, D.G. (1982). „Mechanism of C-terminal amide formation by pituitary enzymes”. Nature (Lond.). 298: 686—688. PMID 7099265.
- ^ Bradbury, A.F. & Smyth, D.G. (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: 579—584. PMID 3691506.
- ^ Glembotski, C.G. (1985). „Further characterization of the peptidyl α-amidating enzyme in rat anterior pituitary secretory granules”. Arch. Biochem. Biophys. 241: 673—683. PMID 2994573.
- ^ Katopodis, A.G., Ping, D. and May, S.W. (1990). „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: 6115—6120. PMID 2207061.
- ^ Murthy, A.S.N., Keutmann, H.T. and Eipper, B.A. (1987). „Further characterization of peptidylglycine α-amidating monooxygenase from bovine neurointermediate pituitary”. Mol. Endocrinol. 1: 290—299. PMID 3453894.
- ^ Murthy, A.S.N., Mains, R.E. and Eipper, B.A. (1986). „Purification and characterization of peptidylglycine α-amidating monooxygenase from bovine neurointermediate pituitary”. J. Biol. Chem. 261: 1815—1822. PMID 3944110.
Literatura
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
- Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze
[уреди | уреди извор]- Peptidylglycine+monooxygenase на US National Library of Medicine Medical Subject Headings (MeSH)
