Cathepsin B-like cysteine proteases of Leishmania mexicana.
A group of Leishmania mexicana cysteine proteases that differ from those previously found in this protozoon are described. The enzymes characteristically have a preference for peptidyl substrates with a phenylalanyl-valyl-arginyl moiety, do not hydrolyse gelatin in substrate-sodium dodecyl sulphate polyacrylamide gels, are stimulated by thiol-reducing agents and are sensitive to inhibitors specific for cysteine proteases. They have unusual solubility properties that indicate that the enzymes are amphiphilic proteins. Two of the cysteine proteases have been purified from L. mexicana amastigotes and shown to have molecular masses of 31 and 33 kDa. Their N-terminal amino acid sequences are very similar and show high homology to the mammalian cysteine protease, cathepsin B.
Robertson
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Department of Zoology, University of Glasgow, Scotland, UK.
Coombs
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D000595:Amino Acid Sequence; D000818:Animals; D002401:Cathepsin B / Q000378:metabolism*; D002850:Chromatography, Gel; D007894:Leishmania mexicana / Q000201:enzymology*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012995:Solubility; D013379:Substrate Specificity
D002401:Cathepsin B