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: Gura_3568
GEB: GM18_3226
GPI: GPICK_06680
DAE: Dtox_4270
MYN: MyAD_25070
MDX: BTO20_03135 BTO20_38200
MSM: MSMEG_6242
MSG: MSMEI_6081
MSB: LJ00_30865
MSN: LI99_30870
MVA: Mvan_5479
ASD: AS9A_4308
NFA: NFA_22240
NFR: ERS450000_01873(thcE)
RER: RER_17770
REY: O5Y_08520
ROP: ROP_61160
RHB: NY08_1972
RRZ: CS378_08140(mdo)
RQI: C1M55_08995(mdo)
GBR: Gbro_1931
GOR: KTR9_1872
GOC: CXX93_15365(mdo)
GIT: C6V83_07720(mdo)
DIZ: CT688_01100(mdo)
SHY: SHJG_2446
NML: Namu_0777
SEN: SACE_2386
AMQ: AMETH_5577(mdo)
PSEA: WY02_13685
PSEH: XF36_28100
 » show all
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 266:3949-54 (1991)
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 212:819-26 (1993)
DOI:10.1111/j.1432-1033.1993.tb17723.x
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 175:1814-22 (1993)
DOI:10.1128/JB.175.6.1814-1822.1993
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 277:46966-73 (2002)
DOI:10.1074/jbc.M207547200
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 156:463-71 (2010)
DOI:10.1099/mic.0.034124-0
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.1.99.37
IUBMB Enzyme Nomenclature: 1.1.99.37
ExPASy - ENZYME nomenclature database: 1.1.99.37
BRENDA, the Enzyme Database: 1.1.99.37

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