Phosphoglucoisomerase: Difference between revisions
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'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red represent highly conserved regions - dark blue regions that are variable) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b). | '''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red represent highly conserved regions - dark blue regions that are variable) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b). | ||
Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in Figure 2 as change in the position of an α helix. | Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in Figure 2 as change in the position of an α helix. | ||
[[Image:Active_site_movement.jpg|thumb|right|'''Fig.2''' Substrate induced movement]] | |||
=='''Mechanism'''== | =='''Mechanism'''== | ||
