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
-
quinoproteins
-
pyrroloquinoline
- methylophilus
- denitrificans
-
paracoccus
- methylotrophus
-
half-reaction
-
linewidth
-
quinone-dependent
-
methylobacterium
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protiated
-
wurster
-
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
results (
results (Results
in table
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459
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20
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125
Engineering
Engineering on EC 1.1.2.7 - methanol dehydrogenase (cytochrome c)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
additional information
additional information
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preparation of an inactive Ca2+-free MDH-containing Hyphomicrobium denitrificans strain, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, elucidation of the Ca2+ ion elimination mechanism, overview
additional information
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preparation of an inactive Ca2+-free MDH-containing Hyphomicrobium denitrificans strain, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, elucidation of the Ca2+ ion elimination mechanism, overview
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additional information
a Ca2+-free enzyme mxaA mutant is inactive
additional information
construction of Ca2+-lacking mutant enzymes MoxA-, MoxK-, and MoxL-, which possess a fully oxidized pyrroloquinoline quinone cofactor that is not in the semiquinone form, incubation in a calcium salt solution leads to full restoration of the mutant enzymes, the mutant enzymes show a cofactor binding defect and are insensitive to inhibitor cyclopropanol, comparison of wild-type and mutant enzyme structures, overview
additional information
construction of Ca2+-lacking, catalytically inactive mutant apoenzymes, reconstitution of the active holoenzyme by incorporation of two exogenous Ca2+ into the active sites of the alpha-subunits of the alpha2beta2 tetramer
additional information
mutation of Cys103-Cys104, forming a disulfide brigde, leads to loss of catalytic activity
additional information
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
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a Ca2+-free enzyme mxaA mutant is inactive
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additional information
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construction of Ca2+-lacking mutant enzymes MoxA-, MoxK-, and MoxL-, which possess a fully oxidized pyrroloquinoline quinone cofactor that is not in the semiquinone form, incubation in a calcium salt solution leads to full restoration of the mutant enzymes, the mutant enzymes show a cofactor binding defect and are insensitive to inhibitor cyclopropanol, comparison of wild-type and mutant enzyme structures, overview
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