Succinyl-CoA synthetase: Difference between revisions

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Lucas Hamlow, David Canner, J.D. McClintic, Michal Harel, Wayne Decatur, Alexander Berchansky

Revision as of 23:09, 28 February 2010 view source Lucas Hamlow (talk \| contribs) 21 edits No edit summary ← Older edit		Revision as of 23:20, 28 February 2010 view source Lucas Hamlow (talk \| contribs) 21 edits No edit summary Newer edit →
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	==Structure==		==Structure==
	'''Succinyl-CoA synthetase''' is a tetramer with an active site on each dimer. This can be seen in the Jmol representation (the PDB code is 1CQJ). The two dimers are denoted alpha and beta. A phosphorylated histidine intermediate <scene name='Lucas_Hamlow_sandbox_1/Active_histidine_residue/1'>(HIS 246)</scene> is responsible for the dephosphorylation of ATP and it is suspected that there are other active sites on the beta dimer that are responsible for the continued catalysis of the reaction.		'''Succinyl-CoA synthetase''' is a tetramer with an active site on each dimer. This can be seen in the Jmol representation (the PDB code is 1CQJ). The two dimers are denoted alpha and beta. A phosphorylated histidine intermediate <scene name='Lucas_Hamlow_sandbox_1/Active_histidine_residue/1'>(HIS 246 alpha)</scene> is responsible for the dephosphorylation of ATP and it is suspected that there are other active sites on the beta dimer that are responsible for the continued catalysis of the reaction. It is theorized that the other active site is in fact two active sites and the HIS 246 beta residue moves between them. A cooperative binding catalysis mechanism has been proposed and it has been shown that binding of ATP at one catalytic site promotes catalytic activity at another catalysis site.