Family C1 cysteine proteases : biological diversity or redundancy?

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DOIResolve DOI: http://doi.org/10.1515/BC.2003.094
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TypeArticle
Journal titleBiological Chemistry
Volume384
Issue6
Pages837843; # of pages: 7
SubjectCysteine; genome; pha; Cathepsin; Papain-like; Peptidase; Specificity
AbstractRecent progress in the identification and partial characterization of novel genes encoding cysteine proteases of the papain family has considerably increased our knowledge of this family of enzymes. Kinetic data available to date for this large family indicate relatively broad, overlapping specificities for most enzymes, thus inspiring a growing conviction that they may exhibit functional redundancy. This is also supported in part by phenotypes of cathepsin knockout mice and suggests that several proteases can substitute for each other to degrade or process a given substrate. On the other hand, specific functions of one particular protease have also been documented. In addition, differences in cellular distribution and intracellular localization may contribute to defining specific functional roles for some of these proteases.
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Note2003300001860423-0014See Contents-PageJournal
Peer reviewedNo
NRC number46190
NPARC number3539452
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Record identifier0ede53f3-e20d-4dae-a6f0-ec0c137a5136
Record created2009-03-01
Record modified2016-05-09
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