Sandbox Reserved 761: Difference between revisions

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[[Image:~~closed~~.jpg|frame|right|Figure 3. When GDH is bound to Glutamate (~~blue~~) it's cleft is closed. ]]

[[Image:ActiveSite.jpg|frame|right|Figure 3. When GDH is not bound to Glutamate it's cleft is open (left). However, when GDH is bound to Glutamate it's cleft is closed (right). ]]

Located on top of the glutamate binding domain, these NAD+ binding domains rotate down upon the substrate and coenzyme to initiate catalysis. The 48-residue antenna that extends from the top of the NAD+ binding domain undergoes conformational changes as the cleft of the active site opens and closes <ref>PMID:12653548</ref>. When GDH is not bound by glutamate its cleft is open, however, when GDH is bound to glutamate it is closed. This position difference between the two domains allows the cleft to be closed, which brings the C4 of the nicotinamide ring and the alpha carbon of the glutamate substrate into the appropriate orientation for a hydride transfer to occur. Residues 200-206, 375-379, and 421-423 are critical for the control of the hinges that open or close the cleft between the two domains <ref>PMID:9405044</ref>. The residues that form this hinge, which allow the cleft to open or close are both near and far from the active site. The <scene name='56/564037/Active_site_final/1'>active site</scene> of GDH is composed of residues: 209-210, 213, 217, 261, 265, 289, 292, 450.

Sandbox Reserved 761: Difference between revisions

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Revision as of 21:31, 5 December 2013 view source Ebony Baldwin (talk \| contribs) 115 edits →Glutamate Dehydrogenase Mechanism ← Older edit		Revision as of 21:36, 5 December 2013 view source Ebony Baldwin (talk \| contribs) 115 edits →Glutamate Dehydrogenase Structure Newer edit →
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	[[Image:~~closed~~.jpg\|frame\|right\|Figure 3. When GDH is bound to Glutamate (~~blue~~) it's cleft is closed. ]]		[[Image:ActiveSite.jpg\|frame\|right\|Figure 3. When GDH is not bound to Glutamate it's cleft is open (left). However, when GDH is bound to Glutamate it's cleft is closed (right). ]]

	Located on top of the glutamate binding domain, these NAD+ binding domains rotate down upon the substrate and coenzyme to initiate catalysis. The 48-residue antenna that extends from the top of the NAD+ binding domain undergoes conformational changes as the cleft of the active site opens and closes <ref>PMID:12653548</ref>. When GDH is not bound by glutamate its cleft is open, however, when GDH is bound to glutamate it is closed. This position difference between the two domains allows the cleft to be closed, which brings the C4 of the nicotinamide ring and the alpha carbon of the glutamate substrate into the appropriate orientation for a hydride transfer to occur. Residues 200-206, 375-379, and 421-423 are critical for the control of the hinges that open or close the cleft between the two domains <ref>PMID:9405044</ref>. The residues that form this hinge, which allow the cleft to open or close are both near and far from the active site. The <scene name='56/564037/Active_site_final/1'>active site</scene> of GDH is composed of residues: 209-210, 213, 217, 261, 265, 289, 292, 450.		Located on top of the glutamate binding domain, these NAD+ binding domains rotate down upon the substrate and coenzyme to initiate catalysis. The 48-residue antenna that extends from the top of the NAD+ binding domain undergoes conformational changes as the cleft of the active site opens and closes <ref>PMID:12653548</ref>. When GDH is not bound by glutamate its cleft is open, however, when GDH is bound to glutamate it is closed. This position difference between the two domains allows the cleft to be closed, which brings the C4 of the nicotinamide ring and the alpha carbon of the glutamate substrate into the appropriate orientation for a hydride transfer to occur. Residues 200-206, 375-379, and 421-423 are critical for the control of the hinges that open or close the cleft between the two domains <ref>PMID:9405044</ref>. The residues that form this hinge, which allow the cleft to open or close are both near and far from the active site. The <scene name='56/564037/Active_site_final/1'>active site</scene> of GDH is composed of residues: 209-210, 213, 217, 261, 265, 289, 292, 450.