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
-
protiated
-
wurster
-
methylomonas
-
one-electron
- extorquens
Reaction
+ 2 ferricytochrome cL = + 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
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Purification
Purification on EC 1.1.2.7 - methanol dehydrogenase (cytochrome c)
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Ca2+-containing and Ca2+-free enzymes from cell-free extracts by ion exchange and hydrophobic interaction chromatography
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native active alpha2beta2 MDH complex by ultracentrifugation, anion echange chromatgraphy, and gel filtration
native enzyme 22fold from strain AM1 in a single cation exchange chromatographical step, followed by ultrafiltration and buffer exchange, over 97% purity
native enzyme 9fold to homogeneity by anion exchange chromatography, ammonium sulfate fractionation, and hydrophobic interaction chromatography, followed by ultrafiltration and gel filtration
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native isozymes by anion exchange chromatography and gel filtration, type I 7.9fold, type II 14.7fold, the lysozyme and freeze-thawing cell disruption method significantly increases the amount of type II MDH in the soluble fraction compared with strong physical disruption methods such as sonication and French Press
recombinant selennomethionine-labeled, detagged MxaJ(residues 12-281) without signal peptide from Escherichia coli strain BL21(DE3) by anion-exchange chromatography and gel filtration
soluble fraction concentrated with Centricon (Millipore, Billerica, Mass, USA), applied to a POROS 20 HQ column, followed by FPLC Superose 12 HR 10/30 column
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