ENZYME entry: EC 1.1.99.37
Accepted Name |
methanol dehydrogenase (nicotinoprotein).
|
Alternative Name(s) |
NDMA-dependent methanol dehydrogenase. |
nicotinoprotein methanol dehydrogenase. |
Reaction catalysed |
A + methanol <=> AH2 + formaldehyde |
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 |
Rhea expert-curated reactions | 1.1.99.37 |
UniProtKB/Swiss-Prot |
|
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