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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Pathway: tryptophan degradation VI (via tryptamine)

Enzyme View:

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: Biosynthesis Secondary Metabolites Biosynthesis Nitrogen-Containing Secondary Compounds Biosynthesis Alkaloids Biosynthesis
Biosynthesis Secondary Metabolites Biosynthesis Nitrogen-Containing Secondary Compounds Biosynthesis
Degradation/Utilization/Assimilation Amino Acids Degradation Tryptophan Degradation

Some taxa known to possess this pathway include ? : Arabidopsis thaliana col , Azospirillum brasilense , Bacillus cereus , Bacillus sp. No. 230 , Brachybacterium conglomeratum , Catharanthus roseus , Enterococcus faecalis , Micrococcus percitreus , Rhizobium phaseoli

Expected Taxonomic Range: Bacteria , Viridiplantae

Summary:
Tryptamine is an important molecule in eukaryotes. In mammals, tryptamine is an endogenous neuroactive metabolite of tryptophan, with behavioral, physiological and pharmacological effects [Mousseau93]. In plants, tryptamine is a merging point of primary and secondary metabolism. Tryptamine, which is derived from tryptophan by the action of tryptophan decarboxylase, provides the indole unit of monoterpenoid-indole and derived alkaloids, many of which are psychoactive [Patten96, Whitmer98]. Tryptophan decarboxylase has been cloned from Catharanthus roseus, and overexpressed in Nicotiana tabacum; it resulted in high tryptamine levels, and resistance to whitefly [Thomas95].

The pathway is widely spread in plants and fungi [Patten96], but little information is available about tryptamine in bacterial metabolism.

Mitoma and Udenfriend [Mitoma60] have demonstrated that strains of Enterococcus faecalis possess tryptophan decarboxylase activity, transforming tryptophan to tryptamine. However, since their enzyme preparation also had tyrosine and phenylalanine decarboxylase activity, and taking into account the very high Km that enzyme had for tryptophan (13 mM) , they were not sure whether tryptophan decarboxylation in that organism was a result of a distinct enzyme or an activity of aromatic L-amino acid decarboxylase (EC 4.1.1.28).

Perley and Stowe [Perley66] demonstrated production of tryptamine from tryptophan by Bacillus cereus strain KVT. The enzyme required pyridoxal phosphate as a cofactor, and had an optimum pH of 8.0. Buki et al [Buki85] isolated and partially purified a tryptophan decarboxylase from another Bacillus strain.

Nakazawa et al detected an aromatic L-amino acid decarboxylase in several bacterial species, which was highly active against tryptophan, forming tryptamine [Nakazawa74, Nakazawa77]. The highest activity was detected in several Micrococcus species. The carboxylase was produced constitutively, but was repressed by high concentrations of tryptamine.

It has been suggested that the soil bacterium Azospirillum brasilense, which lives in association with the roots of grasses and cereals, possesses a pathway for the production of IAA from tryptophan via tryptamine [Hartmann83, CarrenoLopez00]. The organism was able to convert tryptamine, which was added to the growth medium, to IAA, but no enzyme has been identified.

Variants: tryptophan degradation I (via anthranilate) , tryptophan degradation II (via pyruvate) , tryptophan degradation III (eukaryotic) , tryptophan degradation IV (via indole-3-lactate) , tryptophan degradation to 2-amino-3-carboxymuconate semialdehyde , tryptophan degradation V (side chain pathway) , tryptophan degradation VII (via indole-3-pyruvate) , tryptophan degradation VIII (to tryptophol) , tryptophan degradation IX , tryptophan degradation X (mammalian, via tryptamine) , tryptophan degradation XI (mammalian, via kynurenine) , tryptophan degradation XII (Geobacillus)

Unification Links: AraCyc:PWY-3181

Credits:
Created 24-Mar-2005 by Caspi R , SRI International


References

Buki85: Buki KG, Vinh DQ, Horvath I (1985). "Partial purification and some properties of tryptophan decarboxylase from a Bacillus strain." Acta Microbiol Hung 32(1);65-73. PMID: 4036551

CarrenoLopez00: Carreno-Lopez R, Campos-Reales N, Elmerich C, Baca BE (2000). "Physiological evidence for differently regulated tryptophan-dependent pathways for indole-3-acetic acid synthesis in Azospirillum brasilense." Mol Gen Genet 264(4);521-30. PMID: 11129057

Hartmann83: Hartmann, A., Singh, M., Klingmueller, W. (1983). "Isolation and characterization of Azospirillum mutants excreting high amounts of indoleacetic acid." Can. J. Microbiol. 29:916-923.

Mitoma60: Mitoma, C., Udenfriend, S. (1960). "Bacterial tryptophan decarboxylase." Biochim Biophys Acta 37;356-7. PMID: 14423022

Mousseau93: Mousseau DD (1993). "Tryptamine: a metabolite of tryptophan implicated in various neuropsychiatric disorders." Metab Brain Dis 8(1);1-44. PMID: 8098507

Nakazawa74: Nakazawa H, Kumagai H, Yamada H (1974). "Constitutive aromatic L-amino acid decarboxylase from Micrococcus percitreus." Biochem Biophys Res Commun 61(1);75-82. PMID: 4441405

Nakazawa77: Nakazawa, H., Sano, K., Kumagai, H., Yamada, H. (1977). "Distribution and formation of aromatic L-amino acid decarboxylase in bacteria." Agric. Biol.. Chem. 41(11):2241-2247.

Patten96: Patten CL, Glick BR (1996). "Bacterial biosynthesis of indole-3-acetic acid." Can J Microbiol 42(3);207-20. PMID: 8868227

Perley66: Perley JE, Stowe BB (1966). "The production of tryptamine from tryptophan by Bacillus cereus (KVT)." Biochem J 100(1);169-74. PMID: 4960870

Thomas95: Thomas JC, Adams DG, Nessler CL, Brown JK, Bohnert HJ (1995). "Tryptophan Decarboxylase, Tryptamine, and Reproduction of the Whitefly." Plant Physiol 109(2);717-720. PMID: 12228625

Whitmer98: Whitmer S, Canel C, Hallard D, Goncalves C, Verpoorte R (1998). "Influence of Precursor Availability on Alkaloid Accumulation by Transgenic Cell Line of Catharanthus roseus." Plant Physiol 116(2);853-7. PMID: 9490777

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

Bertoldi00: Bertoldi M, Borri Voltattorni C (2000). "Reaction of dopa decarboxylase with L-aromatic amino acids under aerobic and anaerobic conditions." Biochem J 352 Pt 2;533-8. PMID: 11085948

Burkhard01: Burkhard P, Dominici P, Borri-Voltattorni C, Jansonius JN, Malashkevich VN (2001). "Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase." Nat Struct Biol 8(11);963-7. PMID: 11685243

De89: De Luca V, Marineau C, Brisson N (1989). "Molecular cloning and analysis of cDNA encoding a plant tryptophan decarboxylase: comparison with animal dopa decarboxylases." Proc Natl Acad Sci U S A 86(8);2582-6. PMID: 2704736

Fernandez89: Fernandez, J.A., Owen, T.G., Kurz, W.G.W., De Luca, V.D. (1989). "Immunological detection and quantitation of tryptophan decarboxylase in developing Catharanthus roseus seedlings." Plant Physiol. 91: 79-84.

Ichinose85: Ichinose H, Kojima K, Togari A, Kato Y, Parvez S, Parvez H, Nagatsu T (1985). "Simple purification of aromatic L-amino acid decarboxylase from human pheochromocytoma using high-performance liquid chromatography." Anal Biochem 150(2);408-14. PMID: 4091266

Koiwai00: Koiwai H, Akaba S, Seo M, Komano T, Koshiba T (2000). "Functional expression of two Arabidopsis aldehyde oxidases in the yeast Pichia pastoris." J Biochem (Tokyo) 2000;127(4);659-64. PMID: 10739959

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

LopezMeyer97: Lopez-Meyer M, Nessler CL (1997). "Tryptophan decarboxylase is encoded by two autonomously regulated genes in Camptotheca acuminata which are differentially expressed during development and stress." Plant J 11(6);1167-75. PMID: 9225462

Ma02a: Ma J, Ito A (2002). "Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable and active conformation of rat monoamine oxidase A." J Biochem 131(1);107-11. PMID: 11754741

Ma04a: Ma J, Yoshimura M, Yamashita E, Nakagawa A, Ito A, Tsukihara T (2004). "Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors." J Mol Biol 338(1);103-14. PMID: 15050826

Moore96: Moore PS, Dominici P, Borri Voltattorni C (1996). "Cloning and expression of pig kidney dopa decarboxylase: comparison of the naturally occurring and recombinant enzymes." Biochem J 315 ( Pt 1);249-56. PMID: 8670114

Noe84: Noe, W., Mollenschott, C., Berlin, J. (84). "Tryptophan decarboxylase from Catharanthus roseus cell suspension cultures: purification, molecular and kinetic data of the homogeneous protein." Plant Mol Biol 3: 281-288.

Seo00: Seo M, Peeters AJ, Koiwai H, Oritani T, Marion-Poll A, Zeevaart JA, Koornneef M, Kamiya Y, Koshiba T (2000). "The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in abscisic acid biosynthesis in leaves." Proc Natl Acad Sci U S A 97(23);12908-13. PMID: 11050171

Seo00a: Seo M, Koiwai H, Akaba S, Komano T, Oritani T, Kamiya Y, Koshiba T (2000). "Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana." Plant J 23(4);481-8. PMID: 10972874

Seo98: Seo M, Akaba S, Oritani T, Delarue M, Bellini C, Caboche M, Koshiba T (1998). "Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana." Plant Physiol 1998;116(2);687-93. PMID: 9489015

Tsugeno97: Tsugeno Y, Ito A (1997). "A key amino acid responsible for substrate selectivity of monoamine oxidase A and B." J Biol Chem 272(22);14033-6. PMID: 9162023

Wakagi02: Wakagi T, Fukuda E, Ogawa Y, Kino H, Matsuzawa H (2002). "A novel bifunctional molybdo-enzyme catalyzing both decarboxylation of indolepyruvate and oxidation of indoleacetaldehyde from a thermoacidophilic archaeon, Sulfolobus sp. strain 7." FEBS Lett 510(3);196-200. PMID: 11801253

Yamazaki03: Yamazaki Y, Sudo H, Yamazaki M, Aimi N, Saito K (2003). "Camptothecin biosynthetic genes in hairy roots of Ophiorrhiza pumila: cloning, characterization and differential expression in tissues and by stress compounds." Plant Cell Physiol 44(4);395-403. PMID: 12721380

Yao95: Yao K, De Luca V, Brisson N (1995). "Creation of a Metabolic Sink for Tryptophan Alters the Phenylpropanoid Pathway and the Susceptibility of Potato to Phytophthora infestans." Plant Cell 7(11);1787-1799. PMID: 12242360


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc13.