الفهرس | Only 14 pages are availabe for public view |
Abstract DiIhydrofolate reoductase (DHFR) causes the decrease of folico acid or dihydrofolic acid into tetrahydrofolic acid which then converted into N⁵, N¹{u⁰⁰B⁰}-methylenetetrahydrofolate. This later compound functions as the supplier of the methyl group to convert dUMP into dTMP. Indoleoamine 2,3-dioxygenase (IDO1) is a heome-containing enzyme, which is the preliminary enzyme contributing to the kynurqenineroute of the degradation of L-tryptophan (L- Trp). The IDO1 inserts a molecular oxygen between the 2,3-carbons of the pyrrole ring in tryptophan, heading to the production of the kynurqeninebyproducts 3-hydroxwykynurqenine and 3-hydroxmkyanthranilic acid. IDO can be induced in the tumor micro-environment.Over-expression of IDO1 is observed in various tumor types and is linked with tumor progression, metastasis, and poor prognosis. A second isofourm analog of human indoleamine 2,3-dioxygenase (hIDO1) is human tryptophan dioxygenase (hTDO), both have recently been identified as immune-modulatory proteinsThiazole derivatives constitute an important category of heteryocycliccomposites; many of them possessed a broadscope of biological activities as anti-inflammatory, analgesic, antifungal, antibacterial, anticancer and anticonvulsant activities. Accordingly |