EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.7 | ammonia | ammonia affects the rate-limiting step of breaking of the methyl C-H bond | Methylophilus sp. | |
1.1.2.7 | ammonia | ammonia affects the rate-limiting step of breaking of the methyl C-H bond | Methylorubrum extorquens |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.2.7 | crystal structure analysis | Methylophilus sp. |
1.1.2.7 | crystal structure analysis | Methylorubrum extorquens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.2.7 | additional information | mutation of Cys103-Cys104, forming a disulfide brigde, leads to loss of catalytic activity | Methylorubrum extorquens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.1.2.7 | periplasm | - |
Methylophilus sp. | - |
- |
1.1.2.7 | periplasm | - |
Methylorubrum extorquens | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.7 | Ca2+ | binding structure at the active site, overview | Methylophilus sp. | |
1.1.2.7 | Ca2+ | binding structure at the active site, overview, the active site contains a single Ca2+ ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261 | Methylorubrum extorquens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.2.7 | methanol + ferricytochrome cL | Methylophilus sp. | periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria: methanol, methanol dehydrogenase, cytochrome cL, cytochrome cH, oxidase, oxygen | formaldehyde + ferrocytochrome cL | - |
? | |
1.1.2.7 | methanol + ferricytochrome cL | Methylorubrum extorquens | periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria: methanol, methanol dehydrogenase, cytochrome cL, cytochrome cH, oxidase, oxygen | formaldehyde + ferrocytochrome cL | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.2.7 | Methylophilus sp. | - |
- |
- |
1.1.2.7 | Methylorubrum extorquens | P16027 and P14775 | P16027 (large subunit, alpha) and P14775 (small subunit, beta) | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.2.7 | methanol + ferricytochrome cL | - |
Methylophilus sp. | formaldehyde + ferrocytochrome cL | - |
? | |
1.1.2.7 | methanol + ferricytochrome cL | - |
Methylorubrum extorquens | formaldehyde + ferrocytochrome cL | - |
? | |
1.1.2.7 | methanol + ferricytochrome cL | periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria: methanol, methanol dehydrogenase, cytochrome cL, cytochrome cH, oxidase, oxygen | Methylophilus sp. | formaldehyde + ferrocytochrome cL | - |
? | |
1.1.2.7 | methanol + ferricytochrome cL | periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria: methanol, methanol dehydrogenase, cytochrome cL, cytochrome cH, oxidase, oxygen | Methylorubrum extorquens | formaldehyde + ferrocytochrome cL | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.2.7 | methanol dehydrogenase | - |
Methylophilus sp. |
1.1.2.7 | methanol dehydrogenase | - |
Methylorubrum extorquens |
1.1.2.7 | quinohemoprotein (type II) alcohol dehydrogenase | - |
Methylophilus sp. |
1.1.2.7 | quinohemoprotein (type II) alcohol dehydrogenase | - |
Methylorubrum extorquens |
1.1.5.5 | methanol dehydrogenase | - |
- |
1.1.5.5 | quinohemoprotein (type II) alcohol dehydrogenase | - |
- |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.7 | pyrroloquinoline quinone | PQQ, binding structure at the active site, overview, the active site contains a single Ca2 + ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261 | Methylorubrum extorquens | |
1.1.2.7 | pyrroloquinoline quinone | PQQ, binding structure at the active site | Methylophilus sp. |