EC number:1.14.13.128
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.13.128 |
|---|---|
| Description: | 7-methylxanthine demethylase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.13.128 |
| BRENDA Enzyme Link: | BRENDA 1.14.13.128 |
| KEGG Enzyme Link: | KEGG1.14.13.128 |
| BioCyc Enzyme Link: | BioCyc 1.14.13.128 |
| ExPASy Enzyme Link: | ExPASy1.14.13.128 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.13.128 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.13.128 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.13.128 |
| IntEnz Enzyme Link: | IntEnz 1.14.13.128 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.13.128 |
EC number:1.14.13.128
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:30311 | 7-methylxanthine + H(+) + NADH + O2 = formaldehyde + H2O + NAD(+) + xanthine |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[CH3;+0:9]-[n;H0;+0:10]1:[*:11]:[*:12]:[n;H0;+0:13]:[*:14]:1.[H+;H0:15].[O;H0;+0:16]=[O;H0;+0:17]>>[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:11]1:[*:12]:[nH;+0:13]:[*:14]:[n;H0;+0:10]:1.[CH2;+0:9]=[O;H0;+0:16].[OH2;+0:17] |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids. | Summers RM, Louie TM, Yu CL, Gakhar L, Louie KC, Subramanian M | 2012 Apr | 22328667 |
| Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source. | Summers RM, Louie TM, Yu CL, Subramanian M | 2011 Feb | 20966097 |
| RHEA:30307 | 7-methylxanthine + H(+) + NADPH + O2 = formaldehyde + H2O + NADP(+) + xanthine |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[CH3;+0:9]-[n;H0;+0:10]1:[*:11]:[*:12]:[n;H0;+0:13]:[*:14]:1.[H+;H0:15].[O;H0;+0:16]=[O;H0;+0:17]>>[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:11]1:[*:12]:[nH;+0:13]:[*:14]:[n;H0;+0:10]:1.[CH2;+0:9]=[O;H0;+0:16].[OH2;+0:17] |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids. | Summers RM, Louie TM, Yu CL, Gakhar L, Louie KC, Subramanian M | 2012 Apr | 22328667 |
| Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source. | Summers RM, Louie TM, Yu CL, Subramanian M | 2011 Feb | 20966097 |