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Literature summary extracted from

  • Anthony, C.; Williams, P.
    The structure and mechanism of methanol dehydrogenase (2003), Biochim. Biophys. Acta, 1647, 18-23.
    View publication on PubMed

Activating Compound

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.2.7 crystal structure analysis Methylophilus sp.
1.1.2.7 crystal structure analysis Methylorubrum extorquens

Protein Variants

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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.2.7 periplasm
-
Methylophilus sp.
-
-
1.1.2.7 periplasm
-
Methylorubrum extorquens
-
-

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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
-
?

Organism

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)
-

Substrates and Products (Substrate)

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
-
?

Synonyms

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
-
-

Cofactor

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.