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Hindi Endocrinology & Diabetes ResearchISSN: 2470-7570
Bernard P Hughes Author
Subjects of specialization
Affiliation
working in Centre for Cancer Biology, Australia,Cancer Biology
University of South Australia, School of Pharmacy and Medical Sciences, North Terrace, Adelaide, South Australia, 5000, Australia
Biography
Centre for Cancer Biology, University of South Australia and SA Pathology, Frome Road, Adelaide, SA 5000, Australia University of South Australia, School of Pharmacy and Medical Sciences, North Terrace, Adelaide, South Australia, 5000, Australia
Publications
Editorial Subscription
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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