KEGG   ENZYME: 1.1.99.37Help
Entry
EC 1.1.99.37                Enzyme                                 

Name
methanol dehydrogenase (nicotinoprotein);
NDMA-dependent methanol dehydrogenase;
nicotinoprotein methanol dehydrogenase;
methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With unknown physiological acceptors
BRITE hierarchy
Sysname
methanol:acceptor oxidoreductase
Reaction(IUBMB)
methanol + acceptor = formaldehyde + reduced acceptor [RN:R09553]
Reaction(KEGG)
Substrate
methanol [CPD:C00132];
acceptor [CPD:C00028]
Product
formaldehyde [CPD:C00067];
reduced acceptor [CPD:C00030]
Comment
Contains Zn2+ and Mg2+. 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), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, 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 [1-3]. These enzymes are decameric, and possess a 5-fold symmetry [4]. Some of the enzymes can also dismutate formaldehyde to methanol and formate [5].
History
EC 1.1.99.37 created 2010
Orthology
K17067  
formaldehyde dismutase / methanol dehydrogenase
Genes
GUR: 
GEB: 
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MSM: 
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MSN: 
MSH: 
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GBR: 
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GOQ: 
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Taxonomy
Reference
1  [PMID:1995642]
  Authors
Vonck J, Arfman N, De Vries GE, Van Beeumen J, Van Bruggen EF, Dijkhuizen L
  Title
Electron microscopic analysis and biochemical characterization of a novel methanol dehydrogenase from the thermotolerant Bacillus sp. C1.
  Journal
J. Biol. Chem. 266 (1991) 3949-54.
Reference
2  [PMID:8385013]
  Authors
Van Ophem PW, Van Beeumen J, Duine JA
  Title
Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica.
  Journal
Eur. J. Biochem. 212 (1993) 819-26.
Reference
3  [PMID:8449887]
  Authors
Bystrykh LV, Vonck J, van Bruggen EF, van Beeumen J, Samyn B, Govorukhina NI, Arfman N, Duine JA, Dijkhuizen L
  Title
Electron microscopic analysis and structural characterization of novel NADP(H)-containing methanol: N,N'-dimethyl-4-nitrosoaniline oxidoreductases from  the gram-positive methylotrophic bacteria Amycolatopsis methanolica and Mycobacterium gastri MB19.
  Journal
J. Bacteriol. 175 (1993) 1814-22.
Reference
4  [PMID:12351635]
  Authors
Hektor HJ, Kloosterman H, Dijkhuizen L
  Title
Identification of a magnesium-dependent NAD(P)(H)-binding domain in the nicotinoprotein methanol dehydrogenase from Bacillus methanolicus.
  Journal
J. Biol. Chem. 277 (2002) 46966-73.
Reference
5  [PMID:19875438]
  Authors
Park H, Lee H, Ro YT, Kim YM
  Title
Identification and functional characterization of a gene for the methanol : N,N'-dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain JC1 (DSM 3803).
  Journal
Microbiology. 156 (2010) 463-71.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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