EC number:1.14.17.3
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.17 With reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.17.3 | ||
|---|---|---|---|
| Description: | Peptidylglycine monooxygenase. | ||
| Alternative Name: |
Peptidylglycine alpha-amidating monooxygenase. Peptidylglycine 2-hydroxylase. Peptidyl alpha-amidating enzyme. PAM. | ||
| Prosite: | PDOC00080; | ||
| PDB: |
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| Cath: | 2.120.10.30; 2.60.120.230; 2.60.120.310; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.17.3 |
| BRENDA Enzyme Link: | BRENDA 1.14.17.3 |
| KEGG Enzyme Link: | KEGG1.14.17.3 |
| BioCyc Enzyme Link: | BioCyc 1.14.17.3 |
| ExPASy Enzyme Link: | ExPASy1.14.17.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.17.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.17.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.17.3 |
| IntEnz Enzyme Link: | IntEnz 1.14.17.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.17.3 |
EC number:1.14.17.3
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:21452 | a [peptide]-C-terminal-glycine + L-ascorbate + O2 = a [peptide]-C-terminal-2-hydroxyglycine + H2O + L-dehydroascorbate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[OH;+0:3])=[C;H0;+0:4](-[*:5])-[OH;+0:6].[*:7]-[CH2;+0:8]-[*:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[C;H0;+0:4](-[*:5])=[O;H0;+0:6].[*:7]-[CH;+0:8](-[*:9])-[OH;+0:10].[OH2;+0:11] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase. | Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM | 1997 Nov 14 | 9360928 |
| Stopped-Flow Studies of the Reduction of the Copper Centers Suggest a Bifurcated Electron Transfer Pathway in Peptidylglycine Monooxygenase. | Chauhan S, Hosseinzadeh P, Lu Y, Blackburn NJ | 2016 Apr 5 | 26982589 |
| Differential reactivity between two copper sites in peptidylglycine α-hydroxylating monooxygenase. | Chufán EE, Prigge ST, Siebert X, Eipper BA, Mains RE, Amzel LM | 2010 Nov 10 | 20958070 |
| Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex. | Prigge ST, Eipper BA, Mains RE, Amzel LM | 2004 May 7 | 15131304 |
| A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of alpha-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine alpha-amidating monooxygenase in peptide amidation. | Katopodis AG, Ping D, May SW | 1990 Jul 3 | 2207061 |
| Further characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary. | Murthy AS, Keutmann HT, Eipper BA | 1987 Apr | 3453894 |