Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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: ?

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

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 18.5 on Sun Nov 23, 2014, biocyc14.