Lysosomal cysteine proteases: facts and opportunities.
From their discovery in the first half of the 20th century, lysosomal cysteine proteases have come a long way: from being the enzymes non-selectively degrading proteins in lysosomes to being those responsible for a number of important cellular processes. Some of the features and roles of their structures, specificity, regulation and physiology are discussed.
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Department of Biochemistry and Molecular Biology, J.Stefan Institute, Ljubljana, Slovenia. vito.turk@ijs.si
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D000595:Amino Acid Sequence; D000818:Animals; D002403:Cathepsins / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008247:Lysosomes / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010206:Papain / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D002403:Cathepsins; D003546:Cysteine Endopeptidases; D010206:Papain