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1.1.2.7: methanol dehydrogenase (cytochrome c)

This is an abbreviated version!
For detailed information about methanol dehydrogenase (cytochrome c), go to the full flat file.

Word Map on EC 1.1.2.7

Reaction

a primary alcohol
+ 2 ferricytochrome cL =
an aldehyde
+ 2 ferrocytochrome cL + 2 H+

Synonyms

EC 1.1.99.8, Hd-MDH, MDH, MDH2, MEDH, methanol dehydrogenase, More, mxaF, MxaJ, PQQ-dependent methanol dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenase, QH-ADH, QMDH, quinohemoprotein (type II) alcohol dehydrogenase, quinohemoprotein alcohol dehydrogenase, quinone-dependent alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein dehydrogenase, quinoprotein methanol dehydrogenase, type I MDH, type II MDH

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.2 With a cytochrome as acceptor
                1.1.2.7 methanol dehydrogenase (cytochrome c)

Systematic Name

Systematic Name on EC 1.1.2.7 - methanol dehydrogenase (cytochrome c)

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SYSTEMATIC NAME
IUBMB Comments
methanol:cytochrome c oxidoreductase
A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria. It uses the novel specific cytochrome cL as acceptor. Acts on a wide range of primary alcohols, including ethanol, duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde. Activity is stimulated by ammonia or methylamine. It is usually assayed with phenazine methosulfate. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ. It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c), in having a high affinity for methanol and in having a second essential small subunit (no known function).