This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Degradation/Utilization/Assimilation → Amino Acids Degradation → Proteinogenic Amino Acids Degradation → L-tryptophan Degradation|
This upstream portion of tryptophan degradation is found in many eukaryotes (iincluding all metazoa) and some prokaryotes. The compound aminocarboxymuconate semialdehyde, at which this pathway ends, is a branching point: it can be processed via 2-oxoadipate to be completely degraded to acetyl-CoA and ammonia, it can be channeled to form quinolinate, a precursor for NAD, or, as is the case in certain bacteria, it can be degraded via 2-ketopentenoate.
In mammals this pathway occurs in the cytoplasm.
Superpathways: superpathway of NAD biosynthesis in eukaryotes , NAD biosynthesis II (from tryptophan) , L-tryptophan degradation XI (mammalian, via kynurenine) , L-tryptophan degradation IX , L-tryptophan degradation III (eukaryotic)
Variants: L-tryptophan degradation I (via anthranilate) , L-tryptophan degradation II (via pyruvate) , L-tryptophan degradation IV (via indole-3-lactate) , L-tryptophan degradation V (side chain pathway) , L-tryptophan degradation VI (via tryptamine) , L-tryptophan degradation VII (via indole-3-pyruvate) , L-tryptophan degradation VIII (to tryptophol) , L-tryptophan degradation X (mammalian, via tryptamine) , L-tryptophan degradation XII (Geobacillus)
AlberatiGiani96: Alberati-Giani D, Buchli R, Malherbe P, Broger C, Lang G, Kohler C, Lahm HW, Cesura AM (1996). "Isolation and expression of a cDNA clone encoding human kynureninase." Eur J Biochem 239(2);460-8. PMID: 8706755
AlberatiGiani97: Alberati-Giani D, Cesura AM, Broger C, Warren WD, Rover S, Malherbe P (1997). "Cloning and functional expression of human kynurenine 3-monooxygenase." FEBS Lett 410(2-3);407-12. PMID: 9237672
Austin09: Austin CJ, Astelbauer F, Kosim-Satyaputra P, Ball HJ, Willows RD, Jamie JF, Hunt NH (2009). "Mouse and human indoleamine 2,3-dioxygenase display some distinct biochemical and structural properties." Amino Acids 36(1);99-106. PMID: 18274832
Basran08: Basran J, Rafice SA, Chauhan N, Efimov I, Cheesman MR, Ghamsari L, Raven EL (2008). "A kinetic, spectroscopic, and redox study of human tryptophan 2,3-dioxygenase." Biochemistry 47(16);4752-60. PMID: 18370401
Breton00: Breton J, Avanzi N, Magagnin S, Covini N, Magistrelli G, Cozzi L, Isacchi A (2000). "Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase." Eur J Biochem 267(4);1092-9. PMID: 10672018
Calderone02: Calderone V, Trabucco M, Menin V, Negro A, Zanotti G (2002). "Cloning of human 3-hydroxyanthranilic acid dioxygenase in Escherichia coli: characterisation of the purified enzyme and its in vitro inhibition by Zn2+." Biochim Biophys Acta 1596(2);283-92. PMID: 12007609
Comings95: Comings DE, Muhleman D, Dietz G, Sherman M, Forest GL (1995). "Sequence of human tryptophan 2,3-dioxygenase (TDO2): presence of a glucocorticoid response-like element composed of a GTT repeat and an intronic CCCCT repeat." Genomics 29(2);390-6. PMID: 8666386
Dai90: Dai W, Gupta SL (1990). "Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA." Biochem Biophys Res Commun 168(1);1-8. PMID: 2109605
Kucharczyk98: Kucharczyk R, Zagulski M, Rytka J, Herbert CJ (1998). "The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis." FEBS Lett 424(3);127-30. PMID: 9539135
Kurnasov03a: Kurnasov O, Goral V, Colabroy K, Gerdes S, Anantha S, Osterman A, Begley TP (2003). "NAD biosynthesis: identification of the tryptophan to quinolinate pathway in bacteria." Chem Biol 10(12);1195-204. PMID: 14700627
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