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Literature summary for 1.1.2.7 extracted from

  • Anthony, C.; Williams, P.
    The structure and mechanism of methanol dehydrogenase (2003), Biochim. Biophys. Acta, 1647, 18-23.
    View publication on PubMed
Search for more literature for 1.1.2.7

Activating Compound

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 (Commentary)

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

Protein Variants

Protein Variants Comment Organism
additional information mutation of Cys103-Cys104, forming a disulfide brigde, leads to loss of catalytic activity Methylorubrum extorquens

Localization

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

Metals/Ions

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Methylophilus sp.
-
-
-
Methylorubrum extorquens P16027 and P14775 P16027 (large subunit, alpha) and P14775 (small subunit, beta)
-

Substrates and Products (Substrate)

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

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

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.