Sandbox Reserved 660: Difference between revisions
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==Enzymatic Mechanism== | ==Enzymatic Mechanism== | ||
[[Image:Mechanism.png | thumb]] | [[Image:Mechanism for zy.png | thumb]] | ||
The enzymaticmechanism begins with the binding of ATP and hydroxycinnamate substrates. The binding results in 4CL1 adopting the catalytic conformation for the adenylate-forming partial reaction, in which the side chain of Lys-523 interacts with and directs the carboxylate group of the bound hydroxycinnamates for the nucleophilic attack of the α-phosphate of ATP, resulting in an AMP-hydroxycinnamate conjugate and a PPi molecule. The release of PPi then propels 4CL1 to the catalytic conformation of the thioester-forming partial reaction. In this conformation, the side chain of His-234 swings aside to allow access of CoA to the AMP-hydroxycinnamate conjugate. The AMP-hydroxycinnamate conjugate and CoA are then catalyzed by side chains of Lys-438 and Gln-443 to form the final thioester product. The C-domain rotates again to expose the substrate binding site, and the thioester and AMP are released[3]. | The enzymaticmechanism begins with the binding of ATP and hydroxycinnamate substrates. The binding results in 4CL1 adopting the catalytic conformation for the adenylate-forming partial reaction, in which the side chain of Lys-523 interacts with and directs the carboxylate group of the bound hydroxycinnamates for the nucleophilic attack of the α-phosphate of ATP, resulting in an AMP-hydroxycinnamate conjugate and a PPi molecule. The release of PPi then propels 4CL1 to the catalytic conformation of the thioester-forming partial reaction. In this conformation, the side chain of His-234 swings aside to allow access of CoA to the AMP-hydroxycinnamate conjugate. The AMP-hydroxycinnamate conjugate and CoA are then catalyzed by side chains of Lys-438 and Gln-443 to form the final thioester product. The C-domain rotates again to expose the substrate binding site, and the thioester and AMP are released[3]. | ||
