Sandbox Reserved 1072: Difference between revisions
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There are 6 conserved key active site residues that surround 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 <ref name="one"/>. | There are 6 conserved key active site residues that surround the <scene name='69/694238/Heme/2'>heme</scene>. These <scene name='69/694238/Active_site/2'>active site</scene> residues are | ||
<scene name='69/694238/Active_site/3'>Arg 104, Trp 107, His 108, His 270, Asp 381</scene> <ref name="one"/>. | |||
<scene name='69/694238/N_terminus/5'>N terminus</scene> | |||
<scene name='69/694238/N_terminus/6'>N terminus stabilization with residues</scene> | |||
In ''hm''CP, which share 55% and 69% identity with ''mt''CP, the heme is buried inside ''Hm''CP-N, and substrate access to the active site is through a narrow channel that prevents access of a large substrate <ref name="three"/>. 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 <ref name="two">PMID: 12628252</ref>. 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. | In ''hm''CP, which share 55% and 69% identity with ''mt''CP, the heme is buried inside ''Hm''CP-N, and substrate access to the active site is through a narrow channel that prevents access of a large substrate <ref name="three"/>. 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 <ref name="two">PMID: 12628252</ref>. 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. | ||
