Sandbox Reserved 321: Difference between revisions
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[[Image:Secondary Structure of inhA.png|thumb|left|Width200Height300|alt=Secondary Structure Succession of inhA. Secondary structure residues are ordered from blue to red.|Secondary structure succession inhA.]] | [[Image:Secondary Structure of inhA.png|thumb|left|Width200Height300|alt=Secondary Structure Succession of inhA. Secondary structure residues are ordered from blue to red.|Secondary structure succession inhA.]] | ||
__TOC__ | __TOC__ | ||
=Introduction= | =Introduction= | ||
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=Function= | =Function in th Mycolic Acid Pathway= | ||
[[Image:Pathway.png|thumb|right|upright=2|alt=Proposed mechanism.|Formulated mechanism of Mycolic acid synthesis as proposed by Wilson et al.<ref name ="Drug Induced Alterations">PMID:10536008</ref>.]] | |||
= | InhA plays a key role in the synthesis of fatty acids, particularly in ''M. tuberculosis'' which has type one fatty acid synthesis (FASI) and type two fatty acid synthesis (FASII) which together funtion in the synthesis of mycolic acids<ref name ="Function of M Tb">PMID:18552191</ref>. The final step in FASII is compleated by InhA which reduces 2-trans-enoyl-ACP's with chain lengths over twelve carbons in a NADP dependent manner where the hydride transfer precedes protonation<ref name ="Function of M Tb"/><ref name ="Roles of T158">PMID:10521269</ref>. | ||
Like all proteins, the specific funtion of InhA is determined by the amino acids present<ref name ="Roles of T158"/>. Specific residues that have been studied include tryrosine 158 (Y158) and lysine 165 (K165)<ref name ="Roles of T158"/>. Y158 playes an important role in alinging the carbonyl substrate, in fact; rotaion about its C -C bond by 60 brings it inot position where it can hydrogen bond to the carbonyl and provide it with electrophilic stabalization<ref name ="Roles of T158"/>. K165 is essential in the binding of the cofactor NADH, for wihout it, even at high concentrations of NADH, the reaction will not proceed<ref name ="Roles of T158"/>. | |||
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=References= | =References= | ||
<References/> | |||
