EC number:1.1.3.17
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.1 Acting on the CH-OH group of donors |
| 1.1.3 With oxygen as acceptor |
| ID: | 1.1.3.17 |
|---|---|
| Description: | Choline oxidase. |
| Cath: | 1.10.1220.110; 3.30.410.40; 4.10.450.10; 3.40.605.10; 3.50.50.60; 3.40.309.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.1.3.17 |
| BRENDA Enzyme Link: | BRENDA 1.1.3.17 |
| KEGG Enzyme Link: | KEGG1.1.3.17 |
| BioCyc Enzyme Link: | BioCyc 1.1.3.17 |
| ExPASy Enzyme Link: | ExPASy1.1.3.17 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.3.17 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.3.17 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.3.17 |
| IntEnz Enzyme Link: | IntEnz 1.1.3.17 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.3.17 |
| RHEA:11536 | choline + H2O + 2 O2 = betaine + H(+) + 2 H2O2 |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[OH;+0:3].[O;H0;+0:4]=[O;H0;+0:5].[O;H0;+0:6]=[O;H0;+0:7].[OH2;+0:8]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[OH;+0:8].[OH;+0:4]-[OH;+0:5].[OH;+0:6]-[OH;+0:7] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| [Antibacterial properties of two conventional and two high copper dental amalgams]. | Günyakti N, Misirligil A, Gökay O | 1989 May | 2637017 |
| On the catalytic mechanism of choline oxidase. | Fan F, Gadda G | 2005 Feb 23 | 15713082 |
| The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase. | Gadda G, Powell NL, Menon P | 2004 Oct 15 | 15369826 |
| Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress tolerance. | Fan F, Ghanem M, Gadda G | 2004 Jan 1 | 14678796 |
| Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis. | Rand T, Halkier T, Hansen OC | 2003 Jun 17 | 12795615 |
| Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. | Waditee R, Tanaka Y, Aoki K, Hibino T, Jikuya H, Takano J, Takabe T, Takabe T | 2003 Feb 14 | 12466265 |