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Literature summary for 1.1.2.7 extracted from

  • Richardson, I.W.; Anthony, C.
    Characterization of mutant forms of the quinoprotein methanol dehydrogenase lacking an essential calcium ion (1992), Biochem. J., 287, 709-715.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.2.7

Protein Variants

Protein Variants Comment Organism
additional information construction of Ca2+-lacking mutant enzymes MoxA-, MoxK-, and MoxL-, which possess a fully oxidized pyrroloquinoline quinone cofactor that is not in the semiquinone form, incubation in a calcium salt solution leads to full restoration of the mutant enzymes, the mutant enzymes show a cofactor binding defect and are insensitive to inhibitor cyclopropanol, comparison of wild-type and mutant enzyme structures, overview Methylorubrum extorquens

Inhibitors

Inhibitors Comment Organism Structure
Cyclopropanol
-
 Methylorubrum extorquens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ one molecule of Ca2+ per enzyme tetramer. Ca2+ is directly or indirectly involved in the biding of pyrroloquinoline quinone. Methanol oxidation mutants MoxA-, K- and L- contain no Ca2+. The MoxA, K and L proteins may be involved in maintaining a high Ca2+ concentration in the periplasm. It is more likely, that they fill a chaperone function, stabilizing a configuration of methanol dehydrogenase which permits incorporation of low concentrations of Ca2+ into the protein Methylorubrum extorquens

Organism

Organism UniProt Comment Textmining
Methylorubrum extorquens P16027 and P14775 P16027 (large subunit, alpha) and P14775 (small subunit, beta)
-
Methylorubrum extorquens NCIMB 9133 P16027 and P14775 P16027 (large subunit, alpha) and P14775 (small subunit, beta)
-

Renatured (Commentary)

Renatured (Comment) Organism
incubation in a calcium salt solution leads to full restoration of the Ca2+-lacking mutant enzymes to active holoenzymes, overview Methylorubrum extorquens

Subunits

Subunits Comment Organism
tetramer alpha2beta2, comparison of wild-type and mutant enzyme structures, overview Methylorubrum extorquens

Synonyms

Synonyms Comment Organism
methanol dehydrogenase
-
 Methylorubrum extorquens
quinoprotein methanol dehydrogenase
-
 Methylorubrum extorquens

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone PQQ, 2 mol of PQQ per mol of enzyme, the cofactor is predominantly in the semiquinone form, binding structure, overview Methylorubrum extorquens