Family C1 cysteine proteases: biological diversity or redundancy?
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.
Nägler
Dorit K
DK
Department of Clinical Chemistry and Clinical Biochemistry, Hospital of Surgery, Ludwig-Maximilians-University, Nussbaumstrasse 20, D-80336 Munich, Germany.
Ménard
Robert
R
D000818:Animals; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000145:classification* / Q000235:genetics / Q000378:metabolism*; D019143:Evolution, Molecular; D017353:Gene Deletion; D014644:Genetic Variation / Q000235:genetics*; D006801:Humans; D017386:Sequence Homology, Amino Acid
D003546:Cysteine Endopeptidases