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Literature summary extracted from

  • Avezoux, A.; Goodwin, M.G.; Anthony, C.
    The role of the novel disulphide ring in the active site of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens (1995), Biochem. J., 307, 735-741.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.1.2.7 additional information a Ca2+-free enzyme mxaA mutant is inactive Methylorubrum extorquens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.2.7 Ca2+ one molecule per enzyme alpha-subunit. Neither the quinone form of pyrroloquinoline quinone, nor the disulfide ring or its reduced form are absolutely essential for calcium incorporation into the active site Methylorubrum extorquens
1.1.2.7 Fe2+ a cytochrome protein Methylorubrum extorquens

Organism

EC Number Organism UniProt Comment Textmining
1.1.2.7 Methylorubrum extorquens P16027 and P14775 P16027 (large subunit, alpha) and P14775 (small subunit, beta)
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1.1.2.7 Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1 P16027 and P14775 P16027 (large subunit, alpha) and P14775 (small subunit, beta)
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.2.7 methanol + ferricytochrome cL the reaction includes an electron transfer from the quinol PQQH2 to the electron acceptor cytochrome CL mediated by the disulfide structure of the active site, the active site of MDH involves Trp243 that forms the base of the active site chamber, and the Cys103-Cys104 disulfide ring and the pyrroloquinoline quinone prosthetic group, which is in the semiquinone form having the oxygen of the C4 carbonyl displaced out of the plane of the ring, overview Methylorubrum extorquens formaldehyde + ferrocytochrome cL
-
 ?
1.1.2.7 methanol + ferricytochrome cL the reaction includes an electron transfer from the quinol PQQH2 to the electron acceptor cytochrome CL mediated by the disulfide structure of the active site, the active site of MDH involves Trp243 that forms the base of the active site chamber, and the Cys103-Cys104 disulfide ring and the pyrroloquinoline quinone prosthetic group, which is in the semiquinone form having the oxygen of the C4 carbonyl displaced out of the plane of the ring, overview Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1 formaldehyde + ferrocytochrome cL
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.2.7 methanol dehydrogenase
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 Methylorubrum extorquens
1.1.5.5 quinoprotein methanol dehydrogenase
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-

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.2.7 20
-
 assay at Methylorubrum extorquens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.2.7 9
-
 assay at Methylorubrum extorquens

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.7 cytochrome cL
-
 Methylorubrum extorquens
1.1.2.7 additional information an NAD(P)-independent enzyme Methylorubrum extorquens
1.1.2.7 pyrroloquinoline quinone PQQ Methylorubrum extorquens