Sandbox Reserved 763: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 145: | Line 145: | ||
===Reaction Pathway=== | ===Reaction Pathway=== | ||
SK is found in the shikimate pathway, which is present in bacteria, fungi, higher plants, algae, and apicomplexan. This pathway serves to convert erythrose-4-phosphate into chorismate. Chorismate is a required intermediate in the biosynthesis of aromatic amino acids and secondary metabolites. Shikimate kinase is the catalyst for the fifth step of the shikimate pathway, where shikimate (SKM) is converted into shikimate-3-phosphate (S3P) and ATP serves as a co-substrate. It has been found experimentally that SK and shikimate binding involves two steps: substrate attaches to binding site in the first step and LID closure occurs in the second step.<ref name="miscinfo" /> As seen to the left, SK catalyzes the transfer of | SK is found in the shikimate pathway, which is present in bacteria, fungi, higher plants, algae, and apicomplexan. This pathway serves to convert erythrose-4-phosphate into chorismate. Chorismate is a required intermediate in the biosynthesis of aromatic amino acids and secondary metabolites. Shikimate kinase is the catalyst for the fifth step of the shikimate pathway, where shikimate (SKM) is converted into shikimate-3-phosphate (S3P) and ATP serves as a co-substrate. It has been found experimentally that SK and shikimate binding involves two steps: substrate attaches to binding site in the first step and LID closure occurs in the second step.<ref name="miscinfo" /> As seen to the left, SK catalyzes the transfer of the γ phosphate group from from ATP to the 3-hydroxyl group of shikimate. This reaction is reversible, though the forward reaction forming S3P is the important reaction in chorismate synthesis. | ||
| Line 194: | Line 194: | ||
Through docking studies, it has been found that <scene name='56/564039/Nsc162535/1'>NSC162535</scene> is a competitive inhibitor for SK.<ref name="compinhibitor" /> This inhibitor causes a shift in the SB domain due to E53 and R132 interacting instead of E53 and R57 as seen in the wild-type. The geometry of the active site is altered, leading to inhibition of SK.<ref name="compinhibitor" /> | Through docking studies, it has been found that <scene name='56/564039/Nsc162535/1'>NSC162535</scene> is a competitive inhibitor for SK.<ref name="compinhibitor" /> This inhibitor causes a shift in the SB domain due to E53 and R132 interacting instead of E53 and R57 as seen in the wild-type. The geometry of the active site is altered, leading to inhibition of SK.<ref name="compinhibitor" /> | ||
==Additional Sites== | |||
Also see [[Shikimate kinase]] for further information. | |||
==References== | ==References== | ||
{{reflist}} | {{reflist}} | ||
