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Hindi Endocrinology & Diabetes ResearchISSN: 2470-7570
Maurizio Costabile Author
Subjects of specialization
Affiliation
Cell Culture ,Flow Cytometry
American Association of Immunologists, Australasian Society for Immunology, Australian Government Office for
Biography
Learning and Teaching, Australian Society for Biochemistry and Molecular Biology, Clute Institute, Flinders University, Higher Education Research and Development Society of Australasia, Member of International Federation of National Teaching Fellows (IFNTF), Online Learning Consortium (OLC), South Australia Excellence Award, South Australian Science Excellence Awards, The University of South Australia, University of Adelaide, University of South Australia, University of South Australia Adelaide South Australia AU
Publications
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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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