Inhibition of cysteine proteinases by Carica papaya cystatin produced in Escherichia coli.
A papaya cystatin (Cst)-encoding cDNA clone was isolated from a papaya leaf cDNA library and the active protein produced in Escherichia coli. The amino-acid sequence reveals a protein of 11,262 Da with over 40% identity to other published plant Cst. Unique features of the papaya Cst include a single Cys residue, variation in the papain-binding region, and the first reported inhibition of papaya proteinase IV by a Cst.
Song
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Department of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg 39406-5043, USA.
Taylor
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M
Baker
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Bateman
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RC
D001483:Base Sequence; D003001:Cloning, Molecular; D015891:Cystatins / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology*; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry*; D018076:DNA, Complementary / Q000235:genetics; D004926:Escherichia coli; D017343:Genes, Plant; D007700:Kinetics; D008969:Molecular Sequence Data; D010945:Plants, Edible / Q000201:enzymology / Q000235:genetics*; D011994:Recombinant Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D015891:Cystatins; D015853:Cysteine Proteinase Inhibitors; D018076:DNA, Complementary; D011994:Recombinant Proteins