Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ammonia | ammonia affects the rate-limiting step of breaking of the methyl C-H bond | Methylophilus sp. | |
ammonia | ammonia affects the rate-limiting step of breaking of the methyl C-H bond | Methylorubrum extorquens |
Crystallization (Comment) | Organism |
---|---|
crystal structure analysis | Methylophilus sp. |
crystal structure analysis | Methylorubrum extorquens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | mutation of Cys103-Cys104, forming a disulfide brigde, leads to loss of catalytic activity | Methylorubrum extorquens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Methylophilus sp. | - |
- |
periplasm | - |
Methylorubrum extorquens | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | binding structure at the active site, overview | Methylophilus sp. | |
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 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? | |
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 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methylophilus sp. | - |
- |
- |
Methylorubrum extorquens | P16027 and P14775 | P16027 (large subunit, alpha) and P14775 (small subunit, beta) | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
methanol + ferricytochrome cL | - |
Methylophilus sp. | formaldehyde + ferrocytochrome cL | - |
? | |
methanol + ferricytochrome cL | - |
Methylorubrum extorquens | formaldehyde + ferrocytochrome cL | - |
? | |
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 | - |
? | |
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 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
methanol dehydrogenase | - |
Methylophilus sp. |
methanol dehydrogenase | - |
Methylorubrum extorquens |
quinohemoprotein (type II) alcohol dehydrogenase | - |
Methylophilus sp. |
quinohemoprotein (type II) alcohol dehydrogenase | - |
Methylorubrum extorquens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
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 | |
pyrroloquinoline quinone | PQQ, binding structure at the active site | Methylophilus sp. |