Sandbox Reserved 1072: Difference between revisions

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[[Image:Mutation_locations.png|300 px|left|thumb|Pink residues represent the location of possible mutations. Green residues represent the active site. Asp 137 is shown in blue.]]

Of the active site residues that are involved in enzyme catalyzed activation of INH, only His 108 has been a site for mutations that can increase resistance to INH. His 108 has been reported to mutate to glutamic acid and glutamine. These mutations reduce the affinity for INH but the hydrogen bond donor/acceptor groups of glutamine would still allow INH to bind. However, glutamine wouldn't be able to act as proton shuttle in the way His 108 does in the enzyme-catalyzed activation pathway.

Of the active site residues that are involved in enzyme catalyzed activation of INH, only His 108 has been a site for mutations that can increase resistance to INH. His 108 has been reported to mutate to glutamic acid and [http://en.wikipedia.org/wiki/Glutamine glutamine]. These mutations reduce the affinity for INH but the hydrogen bond donor/acceptor groups of glutamine would still allow INH to bind. However, glutamine wouldn't be able to act as proton shuttle in the way His 108 does in the enzyme-catalyzed activation pathway.

No known mutants have been reported to occur at Asp 137, although a few mutants nearby could cause local conformational changes and thereby altering the orientation of the Asp 137 side chain, making it less effective in binding and activation of INH (1).

Sandbox Reserved 1072: Difference between revisions

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@@ Line 47: / Line 47: @@
 [[Image:Mutation_locations.png|300 px|left|thumb|Pink residues represent the location of possible mutations.  Green residues represent the active site. Asp 137 is shown in blue.]]
-Of the active site residues that are involved in enzyme catalyzed activation of INH, only His 108 has been a site for mutations that can increase resistance to INH. His 108 has been reported to mutate to glutamic acid and glutamine. These mutations reduce the affinity for INH but the hydrogen bond donor/acceptor groups of glutamine would still allow INH to bind.  However, glutamine wouldn't be able to act as proton shuttle in the way His 108 does in the enzyme-catalyzed activation pathway.
+Of the active site residues that are involved in enzyme catalyzed activation of INH, only His 108 has been a site for mutations that can increase resistance to INH. His 108 has been reported to mutate to glutamic acid and [http://en.wikipedia.org/wiki/Glutamine glutamine]. These mutations reduce the affinity for INH but the hydrogen bond donor/acceptor groups of glutamine would still allow INH to bind.  However, glutamine wouldn't be able to act as proton shuttle in the way His 108 does in the enzyme-catalyzed activation pathway.
 No known mutants have been reported to occur at Asp 137, although a few mutants nearby could cause local conformational changes and thereby altering the orientation of the Asp 137 side chain, making it less effective in binding and activation of INH (1).