Crystallization (Comment) | Organism |
---|---|
purified enzyme, 5 mg/mL protein in 50 mM Tris-HCl, pH 8.25, and 13.5% PEG 8000, mixed with crystallization solution containing 1 and 50 mM methanol resulting in crystal forms A, B or C with or without incorporated methanol or ethanool, 20°C, X--ray diffraction structure determination and analysis at 1.5-3.0 A resolution, molecular modeling | Methylophilus methylotrophus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | two Ca2+ ions per enzyme tetramer, essential for the enzymatic activity | Methylophilus methylotrophus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
a primary alcohol + 2 ferricytochrome cL | Methylophilus methylotrophus | - |
an aldehyde + 2 ferrocytochrome cL + 2 H+ | - |
? | |
a primary alcohol + 2 ferricytochrome cL | Methylophilus methylotrophus W3A1 | - |
an aldehyde + 2 ferrocytochrome cL + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methylophilus methylotrophus | P38539 | - |
- |
Methylophilus methylotrophus W3A1 | P38539 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ | chemical structure of pyrroloquinoline quinone and hydride transfer mechanism of the enzymatic reaction catalyzed by MEDH, overview | Methylophilus methylotrophus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
a primary alcohol + 2 ferricytochrome cL | - |
Methylophilus methylotrophus | an aldehyde + 2 ferrocytochrome cL + 2 H+ | - |
? | |
a primary alcohol + 2 ferricytochrome cL | - |
Methylophilus methylotrophus W3A1 | an aldehyde + 2 ferrocytochrome cL + 2 H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterotetramer | alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits | Methylophilus methylotrophus |
More | three-dimensional structrue determination of MEDH with bound methanol or ethanol, overview | Methylophilus methylotrophus |
Synonyms | Comment | Organism |
---|---|---|
MEDH | - |
Methylophilus methylotrophus |
methanol dehydrogenase | - |
Methylophilus methylotrophus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyrroloquinoline quinone | the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview | Methylophilus methylotrophus |
General Information | Comment | Organism |
---|---|---|
additional information | the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, which catalyzes the oxidation of methanol to formaldehyde, active site structure with pyrroloquinoline quinone and Ca2+, substrate binding structure, overview | Methylophilus methylotrophus |