ENZYME entry: EC 1.1.99.37
| Accepted Name |
|---|
| NDMA-dependent methanol dehydrogenase.
|
| Alternative Name(s) |
|---|
| Nicotinoprotein methanol dehydrogenase. |
| Reaction catalysed |
|---|
| Methanol + N,N-dimethyl-4-nitrosoaniline <=> formaldehyde + 4-(hydroxylamino)-N,N-dimethylaniline |
| Cofactor(s) |
|---|
| Magnesium; Zinc.
|
| Comment(s) |
|---|
- Nicotinoprotein methanol dehydrogenases have a tightly bound
NADP+/NADPH cofactor that does not dissociate during the catalytic
process.
- Instead, the cofactor is regenerated by a second substrate or
electron carrier.
- While the in vivo electron acceptor is not known, N,N-dimethyl-4-
nitrosoaniline (NDMA) can serve this function in vitro.
- The enzyme has been detected in several Gram-positive methylotrophic
bacteria, including Amycolatopsis methanolica, Rhodococcus
rhodochrous and Rhodococcus erythropolis.
- These enzymes are decameric, and possess a 5-fold symmetry.
- Some of the enzymes can also dismutate formaldehyde to methanol and
formate.
|
| Cross-references |
|---|
| BRENDA | 1.1.99.37 |
| EC2PDB | 1.1.99.37 |
| ExplorEnz | 1.1.99.37 |
| PRIAM enzyme-specific profiles | 1.1.99.37 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.1.99.37 |
| IUBMB Enzyme Nomenclature | 1.1.99.37 |
| IntEnz | 1.1.99.37 |
| MEDLINE | Find literature relating to 1.1.99.37 |
| MetaCyc | 1.1.99.37 |
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