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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)

Purification

Purification on EC 1.1.2.7 - methanol dehydrogenase (cytochrome c)

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ca2+-containing and Ca2+-free enzymes from cell-free extracts by ion exchange and hydrophobic interaction chromatography
-
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
-
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
A3FJ48; A3FJ51; A3FJ49
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
-