Sandbox Reserved 773: Difference between revisions

Line 57:

[[Image:Histidine Decarboxylase Binding Site.png|thumb|right|Figure 3. Interactions between enzyme HDC and cofactor-substrate PLP-HME at the binding site <ref name=jbc/>.]]

The <scene name='56/564049/Binding/1'>~~Catalytic~~ site</scene> 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 <scene name='56/564049/Hydrophobic/1'>hydrophobic pocket</scene> 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 <scene name='56/564049/Binding/2'>catalytic site</scene> 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 <scene name='56/564049/Hydrophobic/1'>hydrophobic pocket</scene> 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.

Sandbox Reserved 773: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 14:26, 2 December 2013 view source Wesley Yang (talk \| contribs) 185 edits →Cofactor and Substrate Binding Pocket ← Older edit		Revision as of 14:30, 2 December 2013 view source Wesley Yang (talk \| contribs) 185 edits →Cofactor and Substrate Binding Pocket Newer edit →
Line 57:		Line 57:
	[[Image:Histidine Decarboxylase Binding Site.png\|thumb\|right\|Figure 3. Interactions between enzyme HDC and cofactor-substrate PLP-HME at the binding site <ref name=jbc/>.]]		[[Image:Histidine Decarboxylase Binding Site.png\|thumb\|right\|Figure 3. Interactions between enzyme HDC and cofactor-substrate PLP-HME at the binding site <ref name=jbc/>.]]

	The <scene name='56/564049/Binding/1'>~~Catalytic~~ site</scene> 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 <scene name='56/564049/Hydrophobic/1'>hydrophobic pocket</scene> 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 <scene name='56/564049/Binding/2'>catalytic site</scene> 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 <scene name='56/564049/Hydrophobic/1'>hydrophobic pocket</scene> 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.