The Genetics of Aldehyde Oxidase in DROSOPHILA MELANOGASTER
About: This article is published in Genetics.The article was published on 1970-11-01. It has received 88 citations till now. The article focuses on the topics: Aldehyde oxidase & Pyridoxal oxidase.
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TL;DR: One or more molybdenum hydroxylases have been found in organisms as different in complexity as man and bacteria, and in mammal's oxidation of hypoxanthine to xanthine and of x anthine to uric acid are steps in purine catabolism prior to excretion.
Abstract: Publisher Summary This chapter describes the enzymes, xanthine oxidase, xanthine dehydrogenase, aldehyde oxidase, and sulfite oxidase. In addition to the molybdenum hydroxylases, sulfite oxidase is discussed in this chapter, though it contains heme rather than flavin and no iron-sulfur. This is because it contains molybdenum, apparently in a chemical environment within the active center, which is quite like that of the metal in the other enzymes. The term xanthine oxidase is to be taken to refer to the enzyme from milk. The enzymes to be considered are widely distributed. Thus, one or more molybdenum hydroxylases have been found in organisms as different in complexity as man and bacteria. In mammal's oxidation of hypoxanthine to xanthine and of xanthine to uric acid are steps in purine catabolism prior to excretion, uric acid being the end product in primates. Individual humans, genetically deficient in xanthine oxidase, are apparently little the worse for the deficiency. The reduced oxygen derivatives are supposed to be available for coupled oxidation reactions—for example, in drug catabolism. The most obvious objection to this hypothesis is the conclusion, discussed in the chapter, that the dehydrogenase form of the xanthine-oxidizing enzymes is more native than is the oxidase form. It must be conceded that the true role of the enzymes in humans and many other species remains somewhat problematical.
186 citations
TL;DR: The results provide strong direct evidence for rapid evolution of new patterns of gene regulation in this group of organisms and the adaptive significance of these pattern differences is unknown.
Abstract: The tissue and stage specificity of expression of five enzymes was examined by electrophoretic analysis of relative enzyme levels in extracts of 13 larval and adult tissues in 27 species of Hawaiian picture-wingedDrosophila. The developmentally regulated patterns of enzyme expression thus characterized were compared to a modal standard phenotype. About 30% of the pattern features analyzed differed significantly from the standard in one or more species. Many of these regulatory differences are essentially qualitative, with tissue specific differences in enzyme activity in excess of 100 fold for some species pairs. The adaptive significance of these pattern differences is unknown, but the results provide strong direct evidence for rapid evolution of new patterns of gene regulation in this group of organisms.
68 citations
TL;DR: It is suggested that JH, by retarding genetic translation mimics M or bb, affects adult development and eclosion and the pharate pupae were the most sensitive to these agents.
64 citations
TL;DR: Strips of Drosophila melanogaster showing a genetically controlled modification of the developmental program for accumulation of aldehyde oxidase are discovered and it is hoped that this and other similar mutations currently under study will provide some insight into the organization of regulatory loci in the eukaryotic genome.
62 citations
TL;DR: It is found that various mutant strains (ma-l or Aldoxn) which do not produce an active enzyme show about the same tolerance to alcohol as do wild strains.
Abstract: Alcohol dehydrogenase is necessary for ethanol detoxification and metabolic utilization. It has been generally assumed that aldehyde oxidase (AO) produced by the Aldox locus (3–56.7) is necessary for a further transformation of acetaldehyde into acetate. We find that various mutant strains (ma-l or Aldoxn) which do not produce an active enzyme show about the same tolerance to alcohol as do wild strains. This physiological paradox is probably to be explained by the discovery of another locus (not localized) which produced a small amount of AO in all tested strains. The adaptive significance of the genetically polymorphic Aldox locus is probably to be looked for in physiological pathways other than ethanol metabolism.
59 citations