Sandbox Reserved 1071: Difference between revisions

Line 26:

There are 6 conserved key active site residues that suround the <scene name='69/694238/Heme/2'>heme</scene>. These <scene name='69/694238/Active_site/2'>active site</scene> residues are Arg 104, Trp 107, His 108, His 270, Asp 381.

The location of the binding site for isoniazid (INH) is located near the ''δ meso'' heme edge, about 3.8 Å away from the heme iron. This binding site is found within what is considered to be the usual substrate access channel of peroxidases. The reaction between INH and the enzyme must occur from interaction in a binding site intended for the natural substrate (A2). Asp 137 plays a key role in the activation and binding of INH. Asp 137 creates energetically favorable interactions due to its ability to make hydrogen-bond interactions between its carboxylic acid side chain and the pyridinyl N1 of INH.

The location of the binding site for [http://en.wikipedia.org/wiki/Isoniazid isoniazid (INH)] is located near the ''δ meso'' heme edge, about 3.8 Å away from the heme iron. This binding site is found within what is considered to be the usual substrate access channel of peroxidases. The reaction between INH and the enzyme must occur from interaction in a binding site intended for the natural substrate (A2). Asp 137 plays a key role in the activation and binding of INH. Asp 137 creates energetically favorable interactions due to its ability to make hydrogen-bond interactions between its carboxylic acid side chain and the pyridinyl N1 of INH.

[[Image:INH_structure._PNG.PNG|300 px|left|thumb|Chemical Structure of Isoniazid (INH)]]

Sandbox Reserved 1071: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 26: / Line 26: @@
 There are 6 conserved key active site residues that suround the <scene name='69/694238/Heme/2'>heme</scene>.  These <scene name='69/694238/Active_site/2'>active site</scene> residues are Arg 104, Trp 107, His 108, His 270, Asp 381.
-The location of the binding site for isoniazid (INH) is located near the ''δ meso'' heme edge, about 3.8 Å away from the heme iron. This binding site is found within what is considered to be the usual substrate access channel of peroxidases.  The reaction between INH and the enzyme must occur from interaction in a binding site intended for the natural substrate (A2).  Asp 137 plays a key role in the activation and binding of INH.  Asp 137 creates energetically favorable interactions due to its ability to make hydrogen-bond interactions between its carboxylic acid side chain and the pyridinyl N1 of INH.
+The location of the binding site for  [http://en.wikipedia.org/wiki/Isoniazid isoniazid (INH)] is located near the ''δ meso'' heme edge, about 3.8 Å away from the heme iron. This binding site is found within what is considered to be the usual substrate access channel of peroxidases.  The reaction between INH and the enzyme must occur from interaction in a binding site intended for the natural substrate (A2).  Asp 137 plays a key role in the activation and binding of INH.  Asp 137 creates energetically favorable interactions due to its ability to make hydrogen-bond interactions between its carboxylic acid side chain and the pyridinyl N1 of INH.
 [[Image:INH_structure._PNG.PNG|300 px|left|thumb|Chemical Structure of Isoniazid (INH)]]