KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | thermodynamics | Methylophilus methylotrophus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Methylophilus methylotrophus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required for catalytic activity, binding structure, overview | Methylophilus methylotrophus |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Methylophilus methylotrophus | - |
- |
- |
Methylophilus methylotrophus W3A1 | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ | additionelimination 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 | Comment | Organism |
---|---|---|
tetramer | 2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination | Methylophilus methylotrophus |
Synonyms | Comment | Organism |
---|---|---|
MDH | - |
Methylophilus methylotrophus |
methanol dehydrogenase | - |
Methylophilus methylotrophus |
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 |