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| '''<span style="line-height: 1.5em; font-size: 13.28px;">Capases</span>'''
| | See [[Caspases]] |
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| <span style="line-height: 1.5em; font-size: 13.28px;">Capsases belong to a subfamily of </span>[[Proteases|proteases]] known as endopeptidases<span style="line-height: 1.5em; font-size: 13.28px;"> which cleave target </span>[[Protein|proteins]] <span style="line-height: 1.5em; font-size: 13.28px;"> at specific </span>[[Aspartic acid|aspartic acids]]<span style="line-height: 1.5em; font-size: 13.28px;">. They hydrolze petide bonds C-terminally in aspartate residues.<ref>Marks F, Klingmuller U, Muller-Decker K, (2009)fckLRCellular Signalling Processing 1st edition page 465fckLRGarland Science 2009</ref> The caspases have </span>[[Cysteine|cysteine]]<span style="line-height: 1.5em; font-size: 13.28px;"> at their </span>[[Enzyme active site|active site]]<span style="line-height: 1.5em; font-size: 13.28px;"> and are named due to the 'C' for </span>[[Cysteine|cysteine]]<span style="line-height: 1.5em; font-size: 13.28px;"> and the 'asp' for </span>[[Aspartic acid|aspartic acid]]<span style="line-height: 1.5em; font-size: 13.28px;">. Caspases are synthesised in the cell as </span>[[Procaspases|procaspases]]<span style="line-height: 1.5em; font-size: 13.28px;"> </span><ref>Alberts et al (2008) Molecular Biology of the Cell, 6th Edition, New York: Garland Science</ref><span style="line-height: 1.5em; font-size: 13.28px;">.</span>
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| '''Capases and [[Apoptosis|Apoptosis]]'''
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| Capases are responsible for the programmed death of a cell. In their inactive state capases are present as zymogens, precapases or blocked by specific capases inhibitors. When [[Javascript:void(0);/*1448212232783*/|apoptosis]] is triggered the capases activate each other forming a cascade. The signal becomes amplified along the cascade and leads to the death of the cell.
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| === References ===
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| <references /><br>
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Latest revision as of 04:24, 23 November 2015