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Literature summary for 1.1.2.7 extracted from

  • Leopoldini, M.; Russo, N.; Toscano, M.
    The preferred reaction path for the oxidation of methanol by PQQ-containing methanol dehydrogenase: addition-elimination versus hydride-transfer mechanism (2007), Chem. Eur. J., 13, 2109-2117.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information thermodynamics Methylophilus methylotrophus

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Methylophilus methylotrophus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required for catalytic activity, binding structure, overview Methylophilus methylotrophus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
8000
-
2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination Methylophilus methylotrophus
62000
-
2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination Methylophilus methylotrophus

Organism

Organism UniProt Comment Textmining
Methylophilus methylotrophus
-
-
-
Methylophilus methylotrophus W3A1
-
-
-

Reaction

Reaction Comment Organism Reaction ID
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ addition–elimination mechanism and hydride transfer mechanism, the catalytic mechanism, with a tetrahedral intermediate, involves the quinone containing prosthetic group, substrate binding and active site structures, overview, the oxygen atoms of the PQQ are involved in several hydrogen bonds with the residues Glu55, Arg109, Thr153, Ser168, Arg324 and Asn387 Methylophilus methylotrophus

Subunits

Subunits Comment Organism
tetramer 2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination Methylophilus methylotrophus

Synonyms

Synonyms Comment Organism
MDH
-
Methylophilus methylotrophus
methanol dehydrogenase
-
Methylophilus methylotrophus

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104 Methylophilus methylotrophus