MetaCyc Pathway: L-tryptophan degradation to 2-amino-3-carboxymuconate semialdehyde
Inferred from experiment

Enzyme View:

Pathway diagram: L-tryptophan degradation to 2-amino-3-carboxymuconate semialdehyde

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/AssimilationAmino Acids DegradationProteinogenic Amino Acids DegradationL-tryptophan Degradation

Some taxa known to possess this pathway include : Burkholderia cenocepacia J2315, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae

Expected Taxonomic Range: Bacteria , Fungi, Metazoa

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)

Created 07-Sep-2007 by Caspi R, SRI International

References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

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

Ball09: Ball HJ, Yuasa HJ, Austin CJ, Weiser S, Hunt NH (2009). "Indoleamine 2,3-dioxygenase-2; a new enzyme in the kynurenine pathway." Int J Biochem Cell Biol 41(3);467-71. PMID: 18282734

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

Batabyal07: Batabyal D, Yeh SR (2007). "Human tryptophan dioxygenase: a comparison to indoleamine 2,3-dioxygenase." J Am Chem Soc 129(50);15690-701. PMID: 18027945

Brady75: Brady FO (1975). "Tryptophan 2,3-dioxygenase: a review of the roles of the heme and copper cofactors in catalysis." Bioinorg Chem 5(2);167-82. PMID: 178384

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

Brown86: Brown D, Hitchcock MJ, Katz E (1986). "Purification and characterization of kynurenine formamidase activities from Streptomyces parvulus." Can J Microbiol 32(6);465-72. PMID: 2425918

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

Christensen07: Christensen M, Duno M, Lund AM, Skovby F, Christensen E (2007). "Xanthurenic aciduria due to a mutation in KYNU encoding kynureninase." J Inherit Metab Dis 30(2);248-55. PMID: 17334708

Colabroy05: Colabroy KL, Begley TP (2005). "Tryptophan catabolism: identification and characterization of a new degradative pathway." J Bacteriol 187(22);7866-9. PMID: 16267312

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

Hayaishi76: Hayaishi O (1976). "Properties and function of indoleamine 2,3-dioxygenase." J Biochem 79(4);13P-21P. PMID: 931956

Hirata77: Hirata F, Ohnishi T, Hayaishi O (1977). "Indoleamine 2,3-dioxygenase. Characterization and properties of enzyme. O2- complex." J Biol Chem 252(13);4637-42. PMID: 194886

Hitchcock88: Hitchcock MJ, Katz E (1988). "Purification and characterization of tryptophan dioxygenase from Streptomyces parvulus." Arch Biochem Biophys 261(1);148-60. PMID: 3341771

Kadoya92: Kadoya A, Tone S, Maeda H, Minatogawa Y, Kido R (1992). "Gene structure of human indoleamine 2,3-dioxygenase." Biochem Biophys Res Commun 189(1);530-6. PMID: 1449503

Keller10: Keller U, Lang M, Crnovcic I, Pfennig F, Schauwecker F (2010). "The actinomycin biosynthetic gene cluster of Streptomyces chrysomallus: a genetic hall of mirrors for synthesis of a molecule with mirror symmetry." J Bacteriol 192(10);2583-95. PMID: 20304989

King07: King NJ, Thomas SR (2007). "Molecules in focus: indoleamine 2,3-dioxygenase." Int J Biochem Cell Biol 39(12);2167-72. PMID: 17320464

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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