Molecular cloning of cDNA for the 29 kDa proteinase participating in decomposition of the larval fat body during metamorphosis of Sarcophaga peregrina (flesh fly).
A cDNA clone for the 29 kDa proteinase participating in tissue disintegration during metamorphosis of Sarcophaga was isolated. This proteinase, named Sarcophaga cathepsin B, consisted of 256 amino acid residues, and contained three putative N-glycosylation sites. By comparison with other cathepsins B, its unique substrate specificity was partly explained by Ala at position 248.
Takahashi
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Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Kurata
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Natori
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S
D000273:Adipose Tissue / Q000201:enzymology; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002401:Cathepsin B / Q000737:chemistry; D003001:Cloning, Molecular; D016384:Consensus Sequence; D015342:DNA Probes; D018076:DNA, Complementary / Q000378:metabolism*; D004175:Diptera / Q000201:enzymology* / Q000502:physiology; D010450:Endopeptidases / Q000096:biosynthesis* / Q000235:genetics; D004792:Enzyme Precursors / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D006801:Humans; D007814:Larva; D008675:Metamorphosis, Biological / Q000502:physiology*; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009838:Oligodeoxyribonucleotides; D017433:Protein Structure, Secondary; D051381:Rats; D017386:Sequence Homology, Amino Acid
D015342:DNA Probes; D018076:DNA, Complementary; D004792:Enzyme Precursors; D009838:Oligodeoxyribonucleotides; D010450:Endopeptidases; D002401:Cathepsin B