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Literature summary extracted from

  • Anthony, C.
    The quinoprotein dehydrogenases for methanol and glucose (2004), Arch. Biochem. Biophys., 428, 2-9.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.2.7 crystal structure determination Methylophilus sp.
1.1.2.7 X-ray diffraction structure determination Methylorubrum extorquens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.2.7 additional information
-
 additional information steady-state analysis using stopped-flow kinetics, molecular dynamics, overview Methylophilus sp.
1.1.2.7 additional information
-
 additional information steady-state analysis using stopped-flow kinetics, molecular dynamics, overview Methylorubrum extorquens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.2.7 periplasm
-
 Methylophilus sp.
-
-
1.1.2.7 periplasm
-
 Methylorubrum extorquens
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.2.7 Ba2+ can substitute for Ca2+, Ba-MDH has twice the maximum activity of the Ca-MDH but with a much lower affinity for its substrates Methylorubrum extorquens
1.1.2.7 Ca2+ the active site contains a single Ca2+ whose coordination sphere contains PQQ and protein atoms Methylophilus sp.
1.1.2.7 Ca2+ the active site contains a single Ca2+ whose coordination sphere contains PQQ and protein atoms Methylorubrum extorquens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.2.7 8500
-
 2 * 66000 + 2 * 8500, alpha2beta2, crystal structure determination Methylorubrum extorquens
1.1.2.7 66000
-
 2 * 66000 + 2 * 8500, alpha2beta2, crystal structure determination Methylorubrum extorquens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.2.7 methanol + ferricytochrome cL Methylophilus sp. MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol formaldehyde + ferrocytochrome cL
-
 ?
1.1.2.7 methanol + ferricytochrome cL Methylorubrum extorquens MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol formaldehyde + ferrocytochrome cL
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.2.7 Methylophilus sp.
-
-
-
1.1.2.7 Methylorubrum extorquens P16027 and P14775 P16027 (large subunit, alpha) and P14775 (small subunit, beta)
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.2.7 a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ detailed reaction mechanism with direct hydride transfe, Glu177 plays the role of general base catalyst Methylorubrum extorquens
a
1.1.2.7 a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ detailed reaction mechanism with direct hydride transfer Methylophilus sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.2.7 methanol + ferricytochrome cL
-
 Methylophilus sp. formaldehyde + ferrocytochrome cL
-
 ?
1.1.2.7 methanol + ferricytochrome cL
-
 Methylorubrum extorquens formaldehyde + ferrocytochrome cL
-
 ?
1.1.2.7 methanol + ferricytochrome cL MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol Methylophilus sp. formaldehyde + ferrocytochrome cL
-
 ?
1.1.2.7 methanol + ferricytochrome cL MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol Methylorubrum extorquens formaldehyde + ferrocytochrome cL
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.2.7 More the large alpha-subunit has a propeller fold making up a superbarrel of eight radially arranged beta-sheets, i.e. the propeller blades, containing the tryptophan-docking motifs that link together the eight beta-sheets, and the presence in the active site of a unique eight-membered disulfide ring structure formed from adjacent cysteine residues 103 and 104, joined by an atypical non-planar peptide bond Methylorubrum extorquens
1.1.2.7 tetramer 2 * 66000 + 2 * 8500, alpha2beta2, crystal structure determination Methylorubrum extorquens

Synonyms

EC Number Synonyms Comment Organism
1.1.2.7 methanol dehydrogenase
-
 Methylophilus sp.
1.1.2.7 methanol dehydrogenase
-
 Methylorubrum extorquens
1.1.2.7 quinoprotein dehydrogenase
-
 Methylophilus sp.
1.1.2.7 quinoprotein dehydrogenase
-
 Methylorubrum extorquens
1.1.5.5 PQQ methanol dehydrogenase
-
-
1.1.5.5 quinoprotein dehydrogenase
-
-

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.2.7 7
-
 assay at Methylorubrum extorquens

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.7 cytochrome cL
-
 Methylophilus sp.
1.1.2.7 cytochrome cL
-
 Methylorubrum extorquens
1.1.2.7 pyrroloquinoline quinone PQQ, is the only prosthetic group Methylophilus sp.
1.1.2.7 pyrroloquinoline quinone PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview Methylorubrum extorquens