Succinyl-CoA synthetase: Difference between revisions
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==Structure== | ==Structure== | ||
'''Succinyl-CoA synthetase''' is a tetramer with an active site on each subunit. This can be seen in the Jmol representation (the PDB code is 1CQJ). The two subunits 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 is another active site on the beta subunit that is responsible for the continued catalysis of the reaction. There is a suspected nucleotide binding site on the N-terminal of the beta subunit which would imply that there are two active sites roughly 35 A apart from each other and that the HIS 246 alpha loop moves between them during catalysis.<ref>PMID:10353839</ref> | '''Succinyl-CoA synthetase''' is a tetramer with an active site on each subunit. This can be seen in the Jmol representation (the PDB code is 1CQJ). The two subunits 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 is another active site on the beta subunit that is responsible for the continued catalysis of the reaction. There is a suspected nucleotide binding site on the N-terminal of the beta subunit which would imply that there are two active sites roughly 35 A apart from each other and that the HIS 246 alpha loop moves between them during catalysis.<ref>PMID:10353839</ref> | ||
On the alpha subunit it has been shown that <scene name='Lucas_Hamlow_sandbox_1/Active_his_with_glu_208/1'>GLU 208 alpha</scene> interacts with the active HIS 246 alpha residue in the phosphorylated and dephosphorylated enzyme and it is supposed that GLU 197 beta serves a similar purpose on the beta subunit.<ref>PMID:11781092</ref> | On the alpha subunit it has been shown that <scene name='Lucas_Hamlow_sandbox_1/Active_his_with_glu_208/1'>GLU 208 alpha</scene> interacts in some way with the active HIS 246 alpha residue in the phosphorylated and dephosphorylated enzyme and it is supposed that GLU 197 beta serves a similar purpose on the beta subunit.<ref>PMID:11781092</ref> | ||
==Mechanism== | ==Mechanism== | ||
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.<ref>PMID:6997289</ref> It has been shown that the enzyme will bind with ATP in the presence of Mg+2 to form a complex containing 2 ATP residues as well as 2 phosphoric acid residues, after incubation this the complex converts to another one containing 4 phosphoric residues per protein. Only the second complex reacts with succinate and CoA to form the succinyl-CoA complex which then releases as many phosphoric residues as bound succinate.<ref>PMID:570066</ref> | 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.<ref>PMID:6997289</ref> It has been shown that the enzyme will bind with ATP in the presence of Mg+2 to form a complex containing 2 ATP residues as well as 2 phosphoric acid residues, after incubation this the complex converts to another one containing 4 phosphoric residues per protein. Only the second complex reacts with succinate and CoA to form the succinyl-CoA complex which then releases as many phosphoric residues as bound succinate.<ref>PMID:570066</ref> A transfer of the phosphoric residue from the first active site is seen to be coordinate with a transfer of a phosphoric residue to the second active site suggesting again a cooperative binding catalysis. This cooperative catalysis means that the presence of ATP or ADP can be both activating and inhibiting depending on the stage of catalysis they interact with the enzyme. | ||
==Bound Form of Succinyl-CoA synthetase== | ==Bound Form of Succinyl-CoA synthetase== | ||