Disease relevance of SelD

• It is expressed ubiquitously throughout embryogenesis and found to be highly enriched in the developing gut and in the nervous system of the embryo.The SelD-like from Drosophila was purified after expression in Escherichia coli [1].
• Halving the selenophosphate synthetase gene dose confers hypersensitivity to oxidative stress in Drosophila melanogaster [2].

High impact information on SelD

• DIAP1 suppresses ROS-induced apoptosis caused by impairment of the selD/sps1 homolog in Drosophila [3].
• In the latter, however, an amino acid replacement is present within the catalytic domain and lacks selenide-dependent SPS activity [4].
• Because most selenoproteins identified so far are antioxidants, the role of ptuf in cell proliferation through the control of the cellular redox balance is discussed [5].
• SelD homolog from Drosophila lacking selenide-dependent monoselenophosphate synthetase activity [1].
• These results and the fact that selD-like possesses an arginine residue at the position of the essential Cys17 (E. coli nomenclature) indicate that the Drosophila gene exerts a function different from that of the classical selenophosphate synthetases [1].

Chemical compound and disease context of SelD

• The purified protein does not catalyze the selenide-dependent ATP hydrolysis reaction and its gene does not complement a selD lesion in E. coli [1].

Biological context of SelD

• Thus, like vertebrates, Drosophila contains two SPS enzymes one with and one without Sec in its catalytic domain [4].
• In this paper we analyse the expression pattern of patufet during the development of imaginal discs and brain as well as the function of this gene in relation to cell proliferation [5].
• This Drosophila gene, termed selD-like, is located in the cytogenetic interval 50 D/E on the right arm of chromosome 2 [1].
• The class I proteins contain a cysteine or selenocysteine residue in the active site and display selenide-dependent selenophosphate synthetase activity [1].
• Our results strongly suggest that selD haploinsufficiency makes heterozygous flies more sensitive to oxidative stress and add further evidence to the role of selenoproteins as cellular antioxidants [2].

Associations of SelD with chemical compounds

• Selenophosphate synthetase catalyzes the synthesis of selenophosphate which is a selenium donor for Sec biosynthesis [6].

Analytical, diagnostic and therapeutic context of SelD

• Northern blot analysis and in situ hybridization indicate that the ptuf gene is expressed in imaginal discs as well as at different stages of development [7].
• Expression analysis by Northern analysis and RT-PCR indicated Selenophosphate synthetase mRNA is present in promastigote and amastigote stages of parasite [8].

References