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|
Some taxa known to possess this pathway include : Geobacillus thermodenitrificans NG80-2
Expected Taxonomic Range:
Geobacillus thermodenitrificans NG80-2 was isolated from a deep-subsurface oil reservoir in Northern China. This organism degrades L-tryptophan to acetyl-CoA via the intermediates anthranilate and 3-hydroxyanthranilate. While L-tryptophan degradation via 3-hydroxyanthranilate is well documented in eukaryotes (although via a different pathway, as documented in pathway L-tryptophan degradation III (eukaryotic)), this is an unusual route for bacteria [Liu10b].
The key enzyme of the pathway, which converts anthranilate to 3-hydroxyanthranilate, is anthranilate hydroxylase. The gene encoding the protein has been cloned, expressed in Escherichia coli and purified, and was shown to be an FAD-dependent hydroxylase. The GTNG_3160 gene that encodes the enzyme is found in a cluster that also contains two additional genes that encode a riboflavin kinase/FMN adenylyltransferase and an FAD reductase, which together provide FAD for the hydroxylase [Liu10b].
The anthranilate degradation gene cluster (GNTG_3150-GNTG_3164) contains genes for the downstream degradation of 3-hydroxyanthranilate via a meta-cleavage pathway, with great similarity to the genes of Pseudomonas fluorescens KU-7, encoding proteins involved in 2-nitrobenzoate degradation [Hasegawa00]. In addition, the cluster is located adjacent to a tryptophan degradation gene cluster (GNTG_3165-GNTG_3169). However, so far only the function of three of these genes has been verified experimentally ( anthranilate hydroxylase, 3-hydroxyanthranilate 3,4-dioxygenase, and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase) [Liu10b].
Transcription of the studied genes was greatly enhanced (several thousand-fold) when the cells were grown with either anthranilate or L-tryptophan as the sole carbon source (as opposed to growth with sucrose) [Liu10b].
Variants: L-tryptophan degradation II (via pyruvate), L-tryptophan degradation III (eukaryotic), L-tryptophan degradation IV (via indole-3-lactate), L-tryptophan degradation VII (via indole-3-pyruvate), L-tryptophan degradation VIII (to tryptophol), L-tryptophan degradation IX, L-tryptophan degradation to 2-amino-3-carboxymuconate semialdehyde, L-tryptophan degradation V (side chain pathway), L-tryptophan degradation VI (via tryptamine), L-tryptophan degradation X (mammalian, via tryptamine), L-tryptophan degradation XI (mammalian, via kynurenine)
Hasegawa00: Hasegawa Y, Muraki T, Tokuyama T, Iwaki H, Tatsuno M, Lau PC (2000). "A novel degradative pathway of 2-nitrobenzoate via 3-hydroxyanthranilate in Pseudomonas fluorescens strain KU-7." FEMS Microbiol Lett 190(2);185-90. PMID: 11034277
Liu10b: Liu X, Dong Y, Li X, Ren Y, Li Y, Wang W, Wang L, Feng L (2010). "Characterization of the anthranilate degradation pathway in Geobacillus thermodenitrificans NG80-2." Microbiology 156(Pt 2);589-95. PMID: 19942660
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
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
Eguchi84: Eguchi N, Watanabe Y, Kawanishi K, Hashimoto Y, Hayaishi O (1984). "Inhibition of indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase by beta-carboline and indole derivatives." Arch Biochem Biophys 232(2);602-9. PMID: 6431906
Ferrandez97: Ferrandez A, Garcia JL, Diaz E (1997). "Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12." J Bacteriol 1997;179(8);2573-81. PMID: 9098055
Fischer13: Fischer B, Boutserin S, Mazon H, Collin S, Branlant G, Gruez A, Talfournier F (2013). "Catalytic properties of a bacterial acylating acetaldehyde dehydrogenase: evidence for several active oligomeric states and coenzyme A activation upon binding." Chem Biol Interact 202(1-3);70-7. PMID: 23237860
Fukuoka02: Fukuoka S, Ishiguro K, Yanagihara K, Tanabe A, Egashira Y, Sanada H, Shibata K (2002). "Identification and expression of a cDNA encoding human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and "quinolinate hypothesis"." J Biol Chem 277(38);35162-7. PMID: 12140278
Gupta00: Gupta S, Mat-Jan F, Latifi M, Clark DP (2000). "Acetaldehyde dehydrogenase activity of the AdhE protein of Escherichia coli is inhibited by intermediates in ubiquinone synthesis." FEMS Microbiol Lett 182(1);51-5. PMID: 10612730
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