EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.2.7 | 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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.7 | Ca2+ | two Ca2+ ions per enzyme tetramer, essential for the enzymatic activity | Methylophilus methylotrophus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.2.7 | a primary alcohol + 2 ferricytochrome cL | Methylophilus methylotrophus | - |
an aldehyde + 2 ferrocytochrome cL + 2 H+ | - |
? | |
1.1.2.7 | a primary alcohol + 2 ferricytochrome cL | Methylophilus methylotrophus W3A1 | - |
an aldehyde + 2 ferrocytochrome cL + 2 H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.2.7 | Methylophilus methylotrophus | P38539 | - |
- |
1.1.2.7 | Methylophilus methylotrophus W3A1 | P38539 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.1.2.7 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.2.7 | a primary alcohol + 2 ferricytochrome cL | - |
Methylophilus methylotrophus | an aldehyde + 2 ferrocytochrome cL + 2 H+ | - |
? | |
1.1.2.7 | a primary alcohol + 2 ferricytochrome cL | - |
Methylophilus methylotrophus W3A1 | an aldehyde + 2 ferrocytochrome cL + 2 H+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.2.7 | heterotetramer | alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits | Methylophilus methylotrophus |
1.1.2.7 | More | three-dimensional structrue determination of MEDH with bound methanol or ethanol, overview | Methylophilus methylotrophus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.2.7 | MEDH | - |
Methylophilus methylotrophus |
1.1.2.7 | methanol dehydrogenase | - |
Methylophilus methylotrophus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.7 | 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 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.2.7 | 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 |