twitter

MetaCyc Enzyme: cytochrome c-dependent methanol dehydrogenase

Synonyms: methanol dehydrogenase, methanol dehydrogenase (cytochrome c)

Species: Methylobacterium organophilum

Subunit composition of cytochrome c-dependent methanol dehydrogenase = [MxaF]2[MxaI]2
         methanol dehydrogenase large subunit = MxaF
         methanol dehydrogenase small subunit = MxaI

Summary:
Gram-negative methylotrophs oxidize methanol to formaldehyde by a periplasmic methanol dehydrogenase (MDH). MDH is an α2β2 tetramer of large (60- to 67-kDa) and small (8.5-kDa) subunits [Anthony92]. MDH is a quinoprotein, each tetramer contains 2 mol of the cofactor pyrroloquinoline quinone (PQQ). In addition, each tetramer also contains 1 mol of calcium [Davidson85].

Electrons are transferred from MDH to cytochrome cL, an atypical cytochrome that serves as the specific electron acceptor for MDH. Cytochrome cL is then oxidized by a typical class I cytochromec (cytochrome cH), which is also specific for the oxidation of methanol [Anthony92]. The MDH and the two cytochromes are soluble and are located in the periplasm of Gram-negative methylotrophs.

Methanol dehydrogenases are quite similar to each other. Genes cloned from one methylotroph often complement defective genes in another, antibodies produced against an enzyme from one methylotroph cross-react with MDHs from other methylotrophs, and genes cloned from facultative methylotrophs hybridize with DNA from a variety of type I and type II methanotrophs as well as with DNA from methylotrophs that do not use methane [Bastien89].

There are several alternative pathways for the oxidation of methanol: Gram-positive methylotrophs oxidize methanol via an NAD-linked methanol dehydrogenase, and methanol-oxidizing yeast species poccess a methanol oxidase system. These alternative enzymes have not been detected in Gram-negative methanotrophic bacteria.

Locations: periplasmic space

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space


Enzymatic reaction of: alcohol dehydrogenase (cytochrome c-dependent methanol dehydrogenase)

EC Number: 1.1.2.7

a primary alcohol + 2 an oxidized cytochrome cL <=> an aldehyde + 2 a reduced cytochrome cL + 2 H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.


Enzymatic reaction of: methanol dehydrogenase

EC Number: 1.1.2.7

methanol + 2 an oxidized cytochrome cL <=> formaldehyde + 2 a reduced cytochrome cL + 2 H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of C1 compounds oxidation to CO2 , methanol and methylamine oxidation to formaldehyde , methanol oxidation to formaldehyde I

Cofactors or Prosthetic Groups: Ca2+ , pyrroloquinoline quinone


Subunit of cytochrome c-dependent methanol dehydrogenase: methanol dehydrogenase large subunit

Synonyms: MoxF, MxaF

Gene: mxaF Accession Number: G-2987 (MetaCyc)

Unification Links: ModBase:P15279 , Protein Model Portal:P15279 , SMR:P15279 , Swiss-Model:P15279 , UniProt:P15279

Relationship Links: InterPro:IN-FAMILY:IPR001479 , InterPro:IN-FAMILY:IPR002372 , InterPro:IN-FAMILY:IPR011047 , InterPro:IN-FAMILY:IPR017512 , InterPro:IN-FAMILY:IPR018391 , InterPro:IN-FAMILY:IPR027295 , Pfam:IN-FAMILY:PF01011 , Prosite:IN-FAMILY:PS00363 , Prosite:IN-FAMILY:PS00364 , Smart:IN-FAMILY:SM00564


Subunit of cytochrome c-dependent methanol dehydrogenase: methanol dehydrogenase small subunit

Synonyms: MxaI

Gene: mxaI Accession Number: G-2988 (MetaCyc)


References

Anthony92: Anthony C (1992). "The structure of bacterial quinoprotein dehydrogenases." Int J Biochem 24(1);29-39. PMID: 1316294

Bastien89: Bastien, C, Machlin, S, Zhang, Y, Donaldson, K, Hanson, RS "Organization of genes required for the oxidation of methanol to formaldehyde in three type II methylotrophs." Appl. Environ. Microbiol. 1989 55:3124-3130.

Davidson85: Davidson VL, Neher JW, Cecchini G (1985). "The biosynthesis and assembly of methanol dehydrogenase in bacterium W3A1." J Biol Chem 260(17);9642-7. PMID: 3894358


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Wed May 6, 2015, biocyc14.