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Literature summary for 1.1.2.8 extracted from

  • Mutzel, A.; Goerisch, H.
    Quinoprotein ethanol dehydrogenase: preparation of the apo-form and reconstitution with pyrroloquinoline quinone and calcium or strontium(2+) ions (1991), Agric. Biol. Chem., 55, 1721-1726.
No PubMed abstract available

Metals/Ions

Metals/Ions Comment Organism Structure
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. Pseudomonas aeruginosa
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. Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
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Renatured (Commentary)

Renatured (Comment) Organism
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. Pseudomonas aeruginosa