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Previous studies have demonstrated that mammalian thioredoxin reductases play roles in protection against oxidant injury, cell growth and transformation, and the recycling of ascorbate from its oxidized form. A thioredoxin reductase protein (TrxR) genes were cloned from the honeybee, Apis mellifera ...

Previous studies have demonstrated that mammalian thioredoxin reductases play roles in protection against oxidant injury, cell growth and transformation, and the recycling of ascorbate from its oxidized form. A thioredoxin reductase protein (TrxR) genes were cloned from the honeybee, Apis mellifera and Apis cerana. The A. mellifera TrxR (Amtrxr) is 1,674bp long and contains an open reading frame (ORF) of 1,485bp. The Apis cerana TrxR (Actrxr) is 1,620bp long and contains an open reading frame (ORF) of 1,476bp. Thioredoxin reductase (TrxR) is one of the components of thioredoxin system. Thioredoxin reductase use NADPH as electron donor to reduce oxidized thioredoxin. The deduced AmTrxR protein has 491 amino acid residues with a conserved active site (CGPC). And the deduced AcTrxR protein has 494 amino acid residues, respectively. The A. mellifera Cu Zn Souperoxide dismutase (Amsod1) is 532bp long and contains an open reading frame (ORF) of 459bp. The Apis cerana SOD1 (Acsod1) is 474bp long and contains an open reading frame (ORF) of 459bp. The deduced SOD1s protein have 152aa, respectively. Honeybee SOD1s (Amsod1 and Acsod1) possesses the typical metal binding ligands of six histidines and one aspartic acid common to SOD1s. We looked for conserved domains/motifs, generated homologous alignments, and conducted phylogenetic analysis of CuZn SOD (SOD1) and Thioredoxin reductase (TrxR).

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