High impact information on Dox-A3

• We also provide evidence that in addition to microbial products, endogenous signals from dying hemocytes contribute to triggering and/or assembly of the prophenoloxidase-activating cascade, and that this process can be inhibited in vitro and in vivo using the viral apoptotic inhibitor p35 [1].
• Drosophila prophenoloxidase is stored in crystal cells, a specialized class of blood cells from which it is released through cell rupture [1].
• Separation of the three phenol oxidase A component activities on polyacrylamide gels shows that Dox-A2 mutations reduce the activity of only the A2 component [2].
• A masquerade-like serine proteinase homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae [3].
• Based upon both their physical separation and a comparison of their sequences, it is suggested that the A4 gene and the A1, A2, and A3 genes constitute two distinct subfamilies within the genome [4].

Biological context of Dox-A3

• Egg-to-adult and relative viabilities in the variants did not decrease at temperature between 18 and 29 degrees C. Genetic analyses indicated that the genes showing the phenotype of variants are new alleles of Mox and Dox-3 on the second chromosome [5].
• A PCR-based cDNA sequence coding A3 has 2501 bp encoding an open reading frame of 682 amino acid residues [6].
• The structural gene for the A3 proenzyme, Dox-3, was not associated with lz on the X chromosome; it mapped to the right of rdo (53.1) and left of M(2)m in the second linkage group [7].
• The kinetics of the activation reactions was unusual in that the final levels of phenoloxidase activity varied depending on the initial concentrations of the activating enzyme, not those of the prophenoloxidase [8].

Anatomical context of Dox-A3

• Phenol oxidase exists in Drosophila hemolymph as a prophenol oxidase, A1 and A3, that is activated in vivo with a native activating system, AMM-1, by limited proteolysis with time [6].

Associations of Dox-A3 with chemical compounds

• Prophenoloxidases A1 and A3 were activated within 1 sec after addition of 2-propanol [9].
• The two isoforms, A1 and A3, could be separated by ammonium sulfate fractionation [10].
• The rate of inhibition of phenoloxidase by diethyldithiocarbamate and phenylthiocarbamate depended on the concentration of 2-propanol [11].

Other interactions of Dox-A3

• Prophenoloxidases, A1 and A3, in these variants had the same mobilities on native electrophoresis as the wild type [5].

Analytical, diagnostic and therapeutic context of Dox-A3

• The native states of A1 and A3 are considered to be homodimeric, as judged by gel-filtration chromatography [10].
• The molecular weights of the monomers of A1 and A3 were estimated by SDS-PAGE to be 78 and 77 kDa, respectively [10].

References