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Literature summary for 1.1.2.7 extracted from

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

Crystallization (Commentary)

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

KM Value [mM]

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
Ca2+ the active site contains a single Ca2+ whose coordination sphere contains PQQ and protein atoms Methylophilus sp.
Ca2+ the active site contains a single Ca2+ whose coordination sphere contains PQQ and protein atoms Methylorubrum extorquens

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
?
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

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

Reaction

Reaction Comment Organism Reaction ID
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 primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ detailed reaction mechanism with direct hydride transfer Methylophilus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methanol + ferricytochrome cL
-
Methylophilus sp. formaldehyde + ferrocytochrome cL
-
?
methanol + ferricytochrome cL
-
Methylorubrum extorquens formaldehyde + ferrocytochrome cL
-
?
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
-
?
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

Subunits Comment Organism
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
tetramer 2 * 66000 + 2 * 8500, alpha2beta2, crystal structure determination Methylorubrum extorquens

Synonyms

Synonyms Comment Organism
methanol dehydrogenase
-
Methylophilus sp.
methanol dehydrogenase
-
Methylorubrum extorquens
quinoprotein dehydrogenase
-
Methylophilus sp.
quinoprotein dehydrogenase
-
Methylorubrum extorquens

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
cytochrome cL
-
Methylophilus sp.
cytochrome cL
-
Methylorubrum extorquens
pyrroloquinoline quinone PQQ, is the only prosthetic group Methylophilus sp.
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