Caspase: Difference between revisions

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&nbsp;Caspases belong to a family of [[Proteases|proteases]] which cleave target proteins at specific [[Aspartic acid|aspartic acids]]. The caspases have [[Cysteine|Cysteine]] at their [[Enzyme active site|active site]] and are named due to the 'C' for [[Cysteine|cysteine]] and the 'asp' for [[Aspartic acid|aspartic acid]]. Caspases are synthesised in the cell as [[Procaspases|procaspases]].<ref>Alberts et al (2008) Molecular Biology of the Cell, 6th Edition, New York: Garland Science</ref>  
Caspases belong to a family of [[Proteases|proteases]] which cleave target [[protein|proteins]] at specific [[Aspartic acid|aspartic acids]]. The caspases have [[Cysteine|cysteine]] at their [[Enzyme active site|active site]] and are named due to the 'C' for [[Cysteine|cysteine]] and the 'asp' for [[Aspartic acid|aspartic acid]]. Caspases are synthesised in the cell as [[Procaspases|procaspases]]&nbsp;<ref>Alberts et al (2008) Molecular Biology of the Cell, 6th Edition, New York: Garland Science</ref>.<br>  


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Revision as of 21:26, 1 December 2011

Caspases belong to a family of proteases which cleave target proteins at specific aspartic acids. The caspases have cysteine at their active site and are named due to the 'C' for cysteine and the 'asp' for aspartic acid. Caspases are synthesised in the cell as procaspases [1].

References

  1. Alberts et al (2008) Molecular Biology of the Cell, 6th Edition, New York: Garland Science