EC number:1.4.9.1
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.4 Acting on the CH-NH2 group of donors |
| 1.4.9 With a copper protein as acceptor |
| ID: | 1.4.9.1 |
|---|---|
| Description: | Methylamine dehydrogenase (amicyanin). |
| Alternative Name: |
Primary-amine dehydrogenase. Methylamine dehydrogenase. MADH. Amine dehydrogenase. |
| Cath: | 2.130.10.10; 2.60.30.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.4.9.1 |
| BRENDA Enzyme Link: | BRENDA 1.4.9.1 |
| KEGG Enzyme Link: | KEGG1.4.9.1 |
| BioCyc Enzyme Link: | BioCyc 1.4.9.1 |
| ExPASy Enzyme Link: | ExPASy1.4.9.1 |
| EC2PDB Enzyme Link: | EC2PDB 1.4.9.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.4.9.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.4.9.1 |
| IntEnz Enzyme Link: | IntEnz 1.4.9.1 |
| MEDLINE Enzyme Link: | MEDLINE 1.4.9.1 |
| RHEA:30207 | H2O + methylamine + 2 oxidized [amicyanin] = formaldehyde + 2 H(+) + NH4(+) + 2 reduced [amicyanin] |
| RULE(radius=1) | [CH3;+0:1]-[NH2;+0:2].[Cu+2;H0:3].[Cu+2;H0:4].[OH2;+0:5]>>[CH2;+0:1]=[O;H0;+0:5].[Cu+;H0:3].[Cu+;H0:4].[NH3;+0:2] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure. | de Beer R, Duine JA, Frank J, Large PJ | 1980 Apr 25 | 6246962 |
| Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine. | Eady RR, Large PJ | 1968 Jan | 4388687 |