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Peptidilglicin monooksigenaza
Identifikatori
EC broj	1.14.17.3
CAS broj	90597-47-0
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

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

\rightleftharpoons

peptidil(2-hidroksiglicin) + dehidroaskorbat + H₂O

Ovaj enzim sadrži bakar. Peptidilglicini sa neutralnim aminokiselinskim ostatkom u pretposlednjoj poziciji su najbolji supstrati.

Reference

↑ 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. and 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

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). 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 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Vanjske veze

MeSH Peptidylglycine+monooxygenase

[1] 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.

[2] Bradbury, A.F. and 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.

[3] 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.

[4] 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.

[5] 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.

[6] 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.

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