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
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1.1.2.7
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1.1.99.8
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phenazine
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methylamine
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formaldehyde
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hyphomicrobium
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quinoproteins
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pyrroloquinoline
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methylophilus
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denitrificans
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paracoccus
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methylotrophus
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half-reaction
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linewidth
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quinone-dependent
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methylobacterium
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protiated
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wurster
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methylomonas
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one-electron
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extorquens
- 1.1.2.7
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1.1.99.8
- phenazine
- methylamine
- formaldehyde
- hyphomicrobium
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quinoproteins
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pyrroloquinoline
- methylophilus
- denitrificans
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paracoccus
- methylotrophus
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half-reaction
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linewidth
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quinone-dependent
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methylobacterium
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protiated
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wurster
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methylomonas
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one-electron
- extorquens
Reaction
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
1.1.2.7 methanol dehydrogenase (cytochrome c)Advanced search results
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results (Results
in table
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459
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164
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20
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125
Reaction
Reaction on EC 1.1.2.7 - methanol dehydrogenase (cytochrome c)
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
active site structure with bound cofactor, the reduced pyrroloquinoline quinone (PQQ) transfers two electrons in single electron-transfer steps to cytochrome cL, creating a semiquinone form of the prosthetic group after the first electron transfer, electron transfer via enzyme residues Cys104, Asp105, and Asn52
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
additionelimination mechanism and hydride transfer mechanism, the catalytic mechanism, with a tetrahedral intermediate, involves the quinone containing prosthetic group, substrate binding and active site structures, overview, the oxygen atoms of the PQQ are involved in several hydrogen bonds with the residues Glu55, Arg109, Thr153, Ser168, Arg324 and Asn387
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
detailed mechanism of methanol oxidation involving residues Asp297 and Glu171, structure-activity analysis by quantum mechanics and molecular mechanics, QM/MM, selfconsistent-charge density-functional tight-binding, SCC-DFTB, and molecular dynamics, the transition state involves Glu171-CO2- as general base
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
the amino-acid residues related to the active site of MDH, E55, C103, C104, R109, T159, S174, E177, T243, W243, N261, D303, R331, N394, and W476, are completely conserved
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
catalytic mechanism, ping-pong kinetic schemes, and transition state structures, analysis by ab initio quantum mechanical methods, hydride transfer from the Calpha-position of the substrate alcohol or aldehyde directly to the C-5 carbon of PQQ is energetically feasible, detailed overview
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
detailed reaction mechanism with direct hydride transfe, Glu177 plays the role of general base catalyst
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
detailed reaction mechanism with direct hydride transfer
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
chemical structure of pyrroloquinoline quinone and hydride transfer mechanism of the enzymatic reaction catalyzed by MEDH, overview
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
Diplococcus sp.
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
the amino-acid residues related to the active site of MDH, E55, C103, C104, R109, T159, S174, E177, T243, W243, N261, D303, R331, N394, and W476, are completely conserved
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
additionelimination mechanism and hydride transfer mechanism, the catalytic mechanism, with a tetrahedral intermediate, involves the quinone containing prosthetic group, substrate binding and active site structures, overview, the oxygen atoms of the PQQ are involved in several hydrogen bonds with the residues Glu55, Arg109, Thr153, Ser168, Arg324 and Asn387
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
chemical structure of pyrroloquinoline quinone and hydride transfer mechanism of the enzymatic reaction catalyzed by MEDH, overview
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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
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