Background: Glutathione S-transferase Omega has been shown to be associated with Parkinson disease.Results: Drosophila GSTO1 regulates mitochondrial ATP synthase activity in parkin mutants.Conclusion: Drosophila GSTO1 plays a protective role in a Drosophila model of Parkinson disease.Significance: These findings may lead to a better understanding of the molecular mechanism of neuroprotection due to GSTO in Parkinson disease.

Drosophila melanogaster has red eyes. Scientists have been curious about the biosynthesis of the red eye pigments and have completed a number of investigations on these compounds. Scientific contributions made over the past 50 years have improved our understanding of the red eye pigments. Researchers have elucidated the chemical structures of some pigments and have successfully purified and identified the enzymes that participate in the biosynthesis of the red eye pigments. In this article, we will review the characteristics of the Drosophila red eye pigments and of the enzymes and genes involved in its biosynthetic pathway. V C 2013 IUBMB Life, 65(4): [334][335][336][337][338][339][340] 2013

Dihydropterin deaminase, which catalyzes the conversion of 7,8-dihydropterin to 7,8-dihydrolumazine, was purified 5850-fold to apparent homogeneity from Drosophila melanogaster. Its molecular mass was estimated to be 48 kDa by gel filtration and SDS-PAGE, indicating that it is a monomer under native conditions. The pI value, temperature, and optimal pH of the enzyme were 5.5, 40°C, and 7.5, respectively. Interestingly the enzyme had much higher activity for guanine than for 7,8-dihydropterin. The specificity constant (k cat /K m ) for guanine (8.6 ؋ 10 6 M ؊1 ⅐s ؊1 ) was 860-fold higher than that for 7,8-dihydropterin

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AbstractSepiapterin reductase (SR) is a key enzyme involved in the biosynthesis of tetrahydrobiopterin (BH4), an essential cofactor for the synthesis of important biogenic amines, including catecholamines and serotonin. BH4 deficiencies have been implicated in several neurological disorders. Here, we characterized sepiapterin reductase (SR) loss-of-function mutants in Drosophila melanogaster and demonstrated that SR mutations are responsible for hyposensitivity to oxidative stress. Biochemical analysis further revealed that SR activity and BH4 levels in SR mutants were significantly reduced. Furthermore, we showed that the levels of phosphorylated Akt and total Akt protein were increased in SR mutants. Our findings indicate that SR plays an important role in the Akt pathway and that SR mutants will be a valuable tool for investigating the physiological functions of BH4.