Prophenol oxidase isoform A1 was isolated from Drosophila melanogaster （The sequence has been deposited in GenBank data base under accession number AB557586） PHOX-S strain, and its characteristics and activation mec...Prophenol oxidase isoform A1 was isolated from Drosophila melanogaster （The sequence has been deposited in GenBank data base under accession number AB557586） PHOX-S strain, and its characteristics and activation mechanism were determined. The NH2-terminal region of PHOX-S A1 was determined to be comprised of 15 amino acids with the following sequence MTNMKMKMKAMMR. Comparison of an alignment in the known prophenol oxidase protein sequences from Drosophila melanogaster strains showed high homology in the copper-binding sequences at the Cu （A） site of the active center. Limited proteolysis takes place between Arg-50 and Val-51. Therefore, it is concluded that prophenol oxidase PHOX-S protein was evolved at the upstream, but no evolved at the central site in Drosophila melanogaster.展开更多
文摘Prophenol oxidase isoform A1 was isolated from Drosophila melanogaster （The sequence has been deposited in GenBank data base under accession number AB557586） PHOX-S strain, and its characteristics and activation mechanism were determined. The NH2-terminal region of PHOX-S A1 was determined to be comprised of 15 amino acids with the following sequence MTNMKMKMKAMMR. Comparison of an alignment in the known prophenol oxidase protein sequences from Drosophila melanogaster strains showed high homology in the copper-binding sequences at the Cu （A） site of the active center. Limited proteolysis takes place between Arg-50 and Val-51. Therefore, it is concluded that prophenol oxidase PHOX-S protein was evolved at the upstream, but no evolved at the central site in Drosophila melanogaster.
