Proteases: Evolution

Abstract

Human proteases have diverse fold structures, catalytic mechanisms, biochemical functions and evolutionary origins. Most arose by gene duplication, but some arose by horizontal transfer from prokaryotes. Adaptation and diversification of their biological roles have resulted from shifts in substrate specificities, expression patterns and new domain combinations.

Keywords: protease; evolution; gene duplication; domains; structure

Figure 1.

(a) Phylogram of HtrA proteases. (b) Human HtrA1 Q92743 domain and gene structure. (c) Human HtrA2 O43464 domain and gene structure. kb: kilobases; Mb: megabases.

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Further Reading

Clausen T, Southan C and Ehrmann M (2002) The HtrA family of proteases. Implications for protein composition and cell fate. Molecular Cell 10(3): 443–455.

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Web Links

European Bioinformatics Institute InterPro database. A resource for whole‐genome analysis http://www.ebi.ac.uk/interpro/

MEROPS Protease Database. A catalog and structure‐based classification of proteases, with additional information about them http://merops.sanger.ac.uk

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How to Cite close
Southan, Christopher(Apr 2008) Proteases: Evolution. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0006141.pub2]