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Review
. 2008 Nov 7;283(45):30433-7.
doi: 10.1074/jbc.R800035200. Epub 2008 Jul 23.

Proteases: multifunctional enzymes in life and disease

Carlos López-Otín  1 , Judith S Bond
Affiliations
Review

Proteases: multifunctional enzymes in life and disease

Carlos López-Otín et al. J Biol Chem. .
No abstract available

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Figures

FIGURE 1.
FIGURE 1.
Global view of the proteolytic landscape in representative eukaryotic genomes. Proteases from human, mouse, Drosophila, and Arabidopsis are shown distributed in catalytic classes and families of related members. Catalytic classes are indicated as aspartic (A), cysteine (C), threonine (T), and serine (S) proteases and metalloprotease (M), and the associated numbers correspond to the different families of proteases belonging to each catalytic class. For example, there are only five distinct evolutionary families within the aspartic protease class, whereas there are 27 families in the metalloprotease class. The y axis shows the number of individual proteases identified thus far within a family for each specie. For example, for the human aspartic protease family A01, there are five proteases, whereas in Arabidopsis, there are 55 members in this family. Data for human and mouse proteases are from Ref. and the Degradome Database; data for Arabidopsis are from Ref. ; and data for Drosophila are from the MEROPS Database (merops.sanger.ac.uk).
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