Sandbox Reserved 773: Difference between revisions
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== Cofactor and Substrate Binding Pocket == | == Cofactor and Substrate Binding Pocket == | ||
[[Image:Histidine Decarboxylase Binding Site.png|thumb|Figure 4. Interactions between enzyme HDC and cofactor-substrate PLP-HME at the binding site]] | [[Image:Histidine Decarboxylase Binding Site.png|thumb|Figure 4. Interactions between enzyme HDC and cofactor-substrate PLP-HME at the binding site <ref name=jgc/>.]] | ||
The binding pocket for the cofactor PLP and the substrate histidine is located at the large domain. Since Histidine methyl ester (HME) is a substrate analog, PLP-HME can be utilized to demonstrate the binding interaction for the substrate-enzyme transition state at the active site <ref name=jbc/> <ref name=inhibition>PMID:850236</ref>. A one-dimensional representation of PLP-HME residing in the binding pocket can be seen in Figure 3. The hydrophobic pocket of the active site are produced by several hydrophobic amino acids including Trp-72, Tyr-80, Leu-102, Phe-104, Ala-275, Tyr-334, Ile-436 (Figure 3). This hydrophobic pocket allow for the substrate to be protected from the solvent during the catalytic reaction. | The binding pocket for the cofactor PLP and the substrate histidine is located at the large domain. Since Histidine methyl ester (HME) is a substrate analog, PLP-HME can be utilized to demonstrate the binding interaction for the substrate-enzyme transition state at the active site <ref name=jbc/> <ref name=inhibition>PMID:850236</ref>. A one-dimensional representation of PLP-HME residing in the binding pocket can be seen in Figure 3. The hydrophobic pocket of the active site are produced by several hydrophobic amino acids including Trp-72, Tyr-80, Leu-102, Phe-104, Ala-275, Tyr-334, Ile-436 (Figure 3). This hydrophobic pocket allow for the substrate to be protected from the solvent during the catalytic reaction. | ||
