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1.1.2.8: alcohol dehydrogenase (cytochrome c)

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

Word Map on EC 1.1.2.8

Reaction

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

Synonyms

Ca2+-dependent PQQ-ADH, EC 1.1.99.8, EDH, ethanol dehydrogenase, exaA, exaF, PedE, PedH, PpADH, PP_2674, PP_2679, PQQ-ADH, PQQ-alcohol dehydrogenase, PQQ-dependent alcohol dehydrogenase, PQQ-dependent type I alcohol dehydrogenase, PQQ-DH9, pyrroloquinoline quinone ethanol dehydrogenase, pyrroloquinoline quinone-dependent alcohol dehydrogenases, pyrroloquinoline quinone-dependent dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase, pyrroquinoline quinone-dependent alcohol dehydrogenase, quinoprotein alcohol dehydrogenase

ECTree

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

Metals Ions

Metals Ions on EC 1.1.2.8 - alcohol dehydrogenase (cytochrome c)

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
one [2Fe-2S] cluster per enzyme
La3+
-
required, active site-bound, 1.3 mol of La3+ per mol of ExaF protomer, indicating a 1:1 ratio of L3+ to protomer of enzyme
Sr2+
-
incubation of apo-enzyme with Sr2+ and pyrroloquinoline quinone leads to the formation of an active Sr2+-form. The Sr2+ and the Ca2+-forms of the enzyme differ in their absorption spectra. The Sr2+-form is inactivated by trans-l,2-diaminocyclohexane-N,N,N',N'-tetraacetic acid twice as fast as the Ca2+-form.
additional information
-
the enzyme from strain AM1 utilizes La3+ rather than Ca2+ as a cofactor