Drosophila melanogaster alcohol dehydrogenase: mechanism of aldehyde oxidation and dismutation

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Drosophila melanogaster alcohol dehydrogenase: mechanism of aldehyde oxidation and dismutation.

Drosophila alcohol dehydrogenase (Adh) catalyses the oxidation of both alcohols and aldehydes. In the latter case, the oxidation is followed by a reduction of the aldehyde, i.e. a dismutation reaction. At high pH, dismutation is accompanied by a small release of NADH, which is not observed at neutral pH. Previously it has been emphasized that kinetic coefficients obtained by measuring the incre...

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Drosophila melanogaster alcohol dehydrogenase: product-inhibition studies.

The Drosophila melanogaster alleloenzymes AdhS and AdhF have been studied with respect to product inhibition by using the two substrate couples propan-2-ol/acetone and ethanol/acetaldehyde together with the coenzyme couple NAD+/NADH. With both substrate couples the reaction was consistent with an ordered Bi Bi mechanism. The substrates added to the enzyme in a compulsory order, with coenzyme as...

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The metabolism of ethanol-derived acetaldehyde by alcohol dehydrogenase (EC 1.1.1.1) and aldehyde dehydrogenase (EC 1.2.1.3) in Drosophila melanogaster larvae.

Both aldehyde dehydrogenase (ALDH, EC 1.2.1.3) and the aldehyde dehydrogenase activity of alcohol dehydrogenase (ADH, EC 1.1.1.1) were found to coexist in Drosophila melanogaster larvae. The enzymes, however, showed different inhibition patterns with respect to pyrazole, cyanamide and disulphiram. ALDH-1 and ALDH-2 isoenzymes were detected in larvae by electrophoretic methods. Nonetheless, in t...

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Post-translational control of alcohol dehydrogenase levels in Drosophila melanogaster.

A trans-acting regulatory gene that alters in vivo protein levels of alcohol dehydrogenase (ADH) has been mapped to a region of the third chromosome of Drosophila melanogaster. The gene has been found to affect the in vivo stability of ADH protein. It was not found to alter levels of total protein of two other enzymes assayed. The action of the gene over development and its possible mode of con...

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Aldehyde dehydrogenase: kinetics and mechanism.

Blakley, R. L. (1985) in Folates and Pterins (Blakley, R. L. & Benkovic, S. J., eds.), vol. 1 , pp. 191 -253, Wiley, New York Bolin, J. T., Filman, D. J., Matthews, D. A., Hamlin, R. C. & Kraut, J. ( 1982) J. Biol. Chem. 257, 1365013662 Clore, G. M., Gronenborn, A. M., Birdsall, B., Feeney, J. & Roberts, G. C. K. ( 1984) Biochem. J. 2 17,659-666 Feeney, J. (1986) in NMR in Living Systems (Axenr...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1998

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj3290561