ENZYME entry: EC 22.214.171.124
View entry in original ENZYME format
View entry in raw text format (no links)
|Methanol dehydrogenase (nicotinoprotein).
|NDMA-dependent methanol dehydrogenase.|
|Nicotinoprotein methanol dehydrogenase.|
|Methanol + acceptor <=> formaldehyde + reduced acceptor|
- Nicotinoprotein methanol dehydrogenases have a tightly bound
NADP+/NADPH cofactor that does not dissociate during the catalytic
- Instead, the cofactor is regenerated by a second substrate or
- 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
|PRIAM enzyme-specific profiles||126.96.36.199|
|KEGG Ligand Database for Enzyme Nomenclature||188.8.131.52|
|IUBMB Enzyme Nomenclature||184.108.40.206|
|MEDLINE||Find literature relating to 220.127.116.11|
entries corresponding to 1.1.99.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-