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.
Reaction
+ = + 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
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Metals Ions
Metals Ions on EC 1.1.2.8 - alcohol dehydrogenase (cytochrome c)
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Ca2+
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
Ca2+
-
contains one Ca2+ ion per subunit of native enzyme. Treatment with trans-l,2-diaminocyclohexane-N,N,N',N'-tetraacetic acid at 30°C leads to an catalytically inactive apo-form. Upon incubation of the apo-form with Ca2 + and pyrroloquinoline quinone a fully active holo-enzyme is reconstituted. 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.
Ca2+
-
rather loosely bound, necessary for pyrroloquinoline quinone binding and for stability of enzyme
Ca2+
-
the prosthetic group is located in the centre of the superbarrel and is coordinated to a calcium ion.In addition, enzyme contains a second Ca2+-binding site at the N-terminus, which contributes to the stability of the native enzyme