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Hindi Endocrinology & Diabetes ResearchISSN: 2470-7570
Nesrine Kamal Bassal Author
Subjects of specialization
Affiliation
University of South Australia, School of Pharmacy and Medical Sciences, Adelaide, Australia,Adelaide, Australia
The University of South Australia, School of Pharmacy and Medical Sciences, Adelaide, Australia
Biography
School of Pharmacy and Medical Sciences, Adelaide, SA 5000, Australia The University of South Australia, School of Pharmacy and Medical Sciences, Adelaide, Australia Using human acute monocytic leukaemic THP-1 cells and human primary monocytes, this study examined the ability of arachidonic acid
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Tryptophan Metabolism- Indoleamine 2,3-Dioxygenase- Friend and Foe
Author(s): Nesrine Kamal Bassal, Bernard P Hughes and Maurizio Costabile
Tryptophan Metabolism- Indoleamine 2,3-Dioxygenase- Friend and Foe
Indoleamine 2,3-dioxygenase (IDO) (EC 1.13.11.42) is a cytoplasmic, heme-containing enzyme that mediates the initial and rate-limiting step in the oxidative catabolism of the essential amino acid L-tryptophan (L-Trp). Recently, an additional IDO molecule, termed IDO2 has been identified. The gene encoding IDO2 is adjacent to the IDO gene. The IDO2 protein has a different expression profile to IDO and while it is able to metabolize L-Trp, IDO2 has a much higher Km for this substrate. In addition both enzymes differ in their selectivity for some inhibitors. Degradation of L-Trp via IDO leads to the production of several metabolites, including N-formyl-kynurenine and Kynurenine (Kyn).
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