To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https

ENZYME entry: EC

Accepted Name
Methanol dehydrogenase (nicotinoprotein).
Alternative Name(s)
NDMA-dependent methanol dehydrogenase.
Nicotinoprotein methanol dehydrogenase.
Reaction catalysed
Methanol + acceptor <=> formaldehyde + reduced acceptor
Mg(2+); Zn(2+).
  • 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.
PRIAM enzyme-specific profiles1.1.99.37
KEGG Ligand Database for Enzyme Nomenclature1.1.99.37
IUBMB Enzyme Nomenclature1.1.99.37
MEDLINEFind literature relating to

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot 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.-.-.-