Sandbox Reserved 321: Difference between revisions

Line 48:

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"/>.

Sandbox Reserved 321: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 01:49, 1 April 2011 view source Kelly Hrywkiw (talk \| contribs) 155 edits No edit summary ← Older edit		Revision as of 02:01, 1 April 2011 view source Kelly Hrywkiw (talk \| contribs) 155 edits No edit summary Newer edit →
Line 48:		Line 48:

	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>.		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"/>.		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"/>.