Sandbox Reserved 1071

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The location of the binding site for isoniazid (INH) is located near the ''delta meso'' heme edge, about 3.8 A 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. 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 isoniazid (INH) is located near the ''delta meso'' heme edge, about 3.8 A 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. 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.
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[[Image:INH_structure._PNG.PNG|300 px|left|thumb|Figure Legend]]
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[[Image:INH_structure._PNG.PNG|300 px|left|thumb|Chemical Structure of Isoniazid (INH)]]

Revision as of 00:21, 9 April 2015

This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.
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Mycobacterium tuberculosis Catalase-Peroxidase

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