Isocitrate lyase of Mycobacterium tuberculosis is inhibited by quercetin through binding at N-terminus

Shukla, Harish; Kumar, Vikash; Singh, A K; Rastogi, Shivangi; Khan, S R; Siddiqi, M I; Krishnan, M Y; Akhtar, M S

dc.contributor.author	Shukla, Harish
dc.contributor.author	Kumar, Vikash
dc.contributor.author	Singh, A K
dc.contributor.author	Rastogi, Shivangi
dc.contributor.author	Khan, S R
dc.contributor.author	Siddiqi, M I
dc.contributor.author	Krishnan, M Y
dc.contributor.author	Akhtar, M S
dc.date.accessioned	2016-03-15T08:51:03Z
dc.date.available	2016-03-15T08:51:03Z
dc.date.issued	2015
dc.identifier.citation	International Journal of Biological Macromolecules 2015, 78,137–141	en
dc.identifier.uri	http://hdl.handle.net/123456789/1605
dc.description.abstract	Combating tuberculosis requires new therapeutic strategies that not only target the actively dividing bacilli but also the dormant bacilli during persistent infection. Isocitrate lyase (ICL) is a key enzyme of the glyoxylate shunt, crucial for the survival of bacteria in macrophages and mice. MtbICL is considered as one of the potential and attractive drug targets against persistent infection. We report the inhibition of MtbICL by quercetin with IC50 of 3.57 μΜ. In addition, quercetin strongly inhibited the growth of Mtb H37Rv utilizing acetate, rather than glucose as the sole carbon source, suggesting the inhibition of glyoxylate shunt. Quercetin binds at the N-terminus of MtbICL (Kd- 6.68 μM).	en
dc.format.extent	512821 bytes
dc.format.mimetype	application/pdf
dc.language.iso	en	en
dc.relation.ispartofseries	CDRI communication number 8956	en
dc.subject	Isocitrate lyase	en
dc.subject	Quercetin	en
dc.subject	Glyoxylate shunt	en
dc.subject	Mycobacteria	en
dc.subject	Docking	en
dc.title	Isocitrate lyase of Mycobacterium tuberculosis is inhibited by quercetin through binding at N-terminus	en
dc.type	Article	en