Phenol oxidase in Drosophila melanogaster occurs as folded phase precursors designated as prophenol oxidase A1 and A3, and prophenol oxidase is activated with alcohol, especially 2-propanol, within a few minutes as un...Phenol oxidase in Drosophila melanogaster occurs as folded phase precursors designated as prophenol oxidase A1 and A3, and prophenol oxidase is activated with alcohol, especially 2-propanol, within a few minutes as unfolded-phase in vitro. To clarify a common effect of alcohols on proteins and peptides, the extract containing prophenol oxidase protein was prepared. Phenol oxidase activity activated with 2-propanol has been maintained stable at least 24 hours remains as it is. Protein of prophenol oxidase was not denatured opposite hypnoses known as the instability of protein with alcohol. Activated prophenol oxidase with 2-propanol remain enzyme activity with no aggregation, stable, renaturation, and the refolding phenomena occurred around the active phase within the catalytic active center of prophenol oxidase protein in Drosophila melanogaster. This study is important to induce the wide range applications of the effect in many fields for rational drag design.展开更多
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Phenol oxidase in Drosophila melanogaster occurs as folded phase precursors designated as prophenol oxidase A1 and A3, and prophenol oxidase is activated with alcohol, especially 2-propanol, within a few minutes as unfolded-phase in vitro. To clarify a common effect of alcohols on proteins and peptides, the extract containing prophenol oxidase protein was prepared. Phenol oxidase activity activated with 2-propanol has been maintained stable at least 24 hours remains as it is. Protein of prophenol oxidase was not denatured opposite hypnoses known as the instability of protein with alcohol. Activated prophenol oxidase with 2-propanol remain enzyme activity with no aggregation, stable, renaturation, and the refolding phenomena occurred around the active phase within the catalytic active center of prophenol oxidase protein in Drosophila melanogaster. This study is important to induce the wide range applications of the effect in many fields for rational drag design.
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.