aldehyde dehydrogenase (FAD-independent)

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Word Map on EC


an aldehyde
a carboxylate
reduced acceptor


aldehyde oxidase, aldehyde oxidoreductase, AOR, AORDd, BV-AIDH, DgAOR, MOP, MOP molybdenum-containing protein


     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.99 With unknown physiological acceptors
       aldehyde dehydrogenase (FAD-independent)


Crystallization on EC - aldehyde dehydrogenase (FAD-independent)

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crystal structure at 2.25 A resolution
kinetic and X-ray crystallographic study, structures of inactive and activated enzyme. Activation/inactivation is governed by the oxidation state of the dithiolene moiety of the pyranopterin cofactor. Incubation with dithionite plus sulfide in the presence of dioxygen produces hydrogen peroxide not associated with the enzyme activation. The peroxide molecule coordinates to molybdenum in a ny2 fashion inhibiting the enzyme activity
sitting drop vapor diffusion method, using 30% (v/v) 2-propanol, 0.2 M magnesium chloride, and 0.2 M HEPES buffer (pH 7.6)
vapour diffusion on sitting drops using a mixture of purified protein in 10 mM Tris-HCl, pH 7.5, and a crystallization solution of 30% isopropanol as precipitant and 200 mM MgCl2 as additive in 200 mM HEPES, pH 7.6, growth of crystals at 4C takes approx. 3 weeks, crystals diffract to 1.28 A
vapour-diffusion using sitting drops and a reservoir containing 100 mM Hepes, pH 7.5, 200 mM MgCl2 and 30% isopropanol, droplets are prepared by mixing 0.004 ml of a 13 mg/ml protein solution in 10 mM Tris, pH 7.6 with 0.002 ml reservoir solution, single crystals are obtained within 3-6 weeks at 4C, crystals diffract to 3.0 A