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User:Amy Kerzmann/Sandbox 5
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Now compare chymotrypsin to <scene name='User:Amy_Kerzmann/Sandbox_5/Trypsin-wt-triad/1' target='1'>trypsin catalytic triad</scene>. The <scene name='User:Amy_Kerzmann/Sandbox_5/Elastase-triad/2' target='2'>elastase catalytic triad</scene>. | Now compare chymotrypsin to <scene name='User:Amy_Kerzmann/Sandbox_5/Trypsin-wt-triad/1' target='1'>trypsin catalytic triad</scene>. The <scene name='User:Amy_Kerzmann/Sandbox_5/Elastase-triad/2' target='2'>elastase catalytic triad</scene>. | ||
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| + | The <scene name='User:Amy_Kerzmann/Sandbox_5/Trypsin-wt-triad/2'>trypsin binding pocket</scene> contains <font color="FF0000">Asp189</font> to select for positively charged sidechains. | ||
The <scene name='User:Amy_Kerzmann/Sandbox_5/Elastase-triad/4' target='2'>elastase binding pocket</scene> contains <font color="#808080">Gly190</font>, <font color="#008000">Val216</font> and <font color="#FFA500">Thr226</font>. | The <scene name='User:Amy_Kerzmann/Sandbox_5/Elastase-triad/4' target='2'>elastase binding pocket</scene> contains <font color="#808080">Gly190</font>, <font color="#008000">Val216</font> and <font color="#FFA500">Thr226</font>. | ||
| + | |||
| + | ---- | ||
<quiz display=simple> | <quiz display=simple> | ||
{ | { | ||
Revision as of 09:21, 10 February 2010
Serine Proteases
The most famous members of the serine protease family are trypsin, chymotrypsin and elastase. These digestive enzymes are also useful tools in biochemistry and molecular biology to ascertain protein sequences.
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Serine proteases perform their catalytic roles using three key residues: Ser, His, Asp. Because the proteases utilize these three residues for function, they are referred to as the catalytic triad. Highlight the . Mouse over the structure to determine the residue numbers for Ser, Asp and His.
Now compare chymotrypsin to . The .
The contains Asp189 to select for positively charged sidechains.
The contains Gly190, Val216 and Thr226.
