Abstract:
:Recent 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.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Nägler DK,Ménard Rdoi
10.1515/BC.2003.094keywords:
subject
Has Abstractpub_date
2003-06-01 00:00:00pages
837-43issue
6eissn
1431-6730issn
1437-4315journal_volume
384pub_type
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