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B6db activities: 4.1.1.28

4.1.1.28
Description Aromatic-L-amino-acid decarboxylase.
Alternative names AADC;
DOPA decarboxylase;
DDC;
Tryptophan decarboxylase;
Hydroxytryptophan decarboxylase;
Tyrosine decarboxylase (ambiguous);
Phenylacetaldehyde synthase.
Catalyzed reaction L-tryptophan = tryptamine + CO(2).
Cofactor Pyridoxal-phosphate.
Comments -!- Also acts on L-tryptophan, 5-hydroxy-L-tryptophan and dihydroxy- L-phenylalanine (DOPA).
-!- Formerly EC 4.1.1.26 and EC 4.1.1.27.
These enzymes can decarboxylate (with variable efficiency) L-Phenylalanine, L-Tyrosine, L-Histidine, 3,4-Dihydroxy-L-phenylalanine, 5-Hydroxy-L-tryptophan, 5-Hydroxykynurenamine.

In metazoa, aromatic L-amino acid decarboxylase catalyzes the synthesis of biogenic amines, including the neurotransmitters serotonin and dopamine.
Plants contain usually several different proteins with AADC activity, involved in the production of secondary metabolites. Although plant AADCs are close sequence and functional homologs of animal AADCs, the enzymes display significant differences in their substrate specificities. AADCs from mammals and insects accept a broad range of aromatic L-amino acids, whereas plant enzymes exhibit exclusive substrate specificity for L-amino acids with either an indole side chain (Trp decarboxylases) or a phenol side chain (Tyr/Phe decarboxylases), but not both.

Phenylacetaldehyde synthase from petunia is a specialized phenylalanine decarboxylase that is capable of stoichiometrically coupling the decarboxylation of Phe with the further conversion of phenylethylamine to phenylacetaldehyde.

Prosite PROSITE; PDOC00329;
PDB 1JS6; 3RBF; 3RCH;
Organisms -Plants -Metazoa -Human
 

Family 

4.1.1.28 (34)
 
Links Enzyme (activities) 4.1.1.28
BRENDA (activities) 4.1.1.28
KEGG (pathways) 4.1.1.28
PLPMDB (PLP mutants) 4.1.1.28
 
References
 Tossaton Charoonratana, Juraithip Wungsintaweekul , Niwat Keawpradub and Rob Verpoorte2 (2013) Molecular cloning and expression of tryptophan decarboxylase from Mitragyna speciosa Acta Physiologiae Plantarum 35 2611-2621.

 Wang MX, Cai ZZ, Lu Y, Xin HH, Chen RT, Liang S, Singh CO, Kim JN, Niu YS, Miao YG. (2013) Expression and functions of dopa decarboxylase in the silkworm, Bombyx mori was regulated by molting hormone. Mol Biol Rep. 40 4115-22..

 Yuwen L, Zhang FL, Chen QH, Lin SJ, Zhao YL, Li ZY. (2013) The role of aromatic L-amino acid decarboxylase in bacillamide C biosynthesis by Bacillus atrophaeus C89. Sci Rep. 3 .

 Liu W, Chen R, Chen M, Zhang H, Peng M, Yang C, Ming X, Lan X, Liao Z. (2012) Tryptophan decarboxylase plays an important role in ajmalicine biosynthesis in Rauvolfia verticillata. Planta. 236 239-50.

 Gutensohn M, Klempien A, Kaminaga Y, Nagegowda DA, Negre-Zakharov F, Huh JH, Luo H, Weizbauer R, Mengiste T, Tholl D, Dudareva N. (2011) Role of aromatic aldehyde synthase in wounding/herbivory response and flower scent production in different Arabidopsis ecotypes. Plant J. 66 591-602.

 Park S, Kang K, Lee K, Choi D, Kim YS, Back K. (2009) Induction of serotonin biosynthesis is uncoupled from the coordinated induction of tryptophan biosynthesis in pepper fruits (Capsicum annuum) upon pathogen infection. Planta 230 1197-206.

 Kaminaga Y, Schnepp J, Peel G, Kish CM, Ben-Nissan G, Weiss D, Orlova I, Lavie O, Rhodes D, Wood K, Porterfield DM, Cooper AJ, Schloss JV, Pichersky E, Vainstein A, Dudareva N. (2006) Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation J Biol Chem 281 23357-66.

 Hare EE, Loer CM. (2004) Function and evolution of the serotonin-synthetic bas-1 gene and other aromatic amino acid decarboxylase genes in Caenorhabditis BMC Evol Biol 2 24.

 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 44 395-403.

 Burkhard, P.; Dominici, P.; Borri-Voltattorni, C.; Jansonius, J. N.; Malashkevich, V. N. (2001) Structural insight into Parkinson's disease treatment from drug- inhibited DOPA decarboxylase Nat Struct Biol 8 963-7.

 Facchini PJ, Huber-Allanach KL, Tari LW. (2000) Plant aromatic L-amino acid decarboxylases: evolution, biochemistry, regulation, and metabolic engineering applications Phytochemistry 54 121-38.

 Muller, R.; Gerth, K.; Brandt, P.; Blocker, H.; Beyer, S. (2000) Identification of an L-dopa decarboxylase gene from Sorangium cellulosum So ce90 Arch Microbiol 173 303-6.

 Maldonado-Mendoza, I.E.; Lopez-Meyer, M.; Galef, J.R.; Burnett, R.J.; Nessler, C.L. (1996) Molecular analysis of a new member of the opium poppy tyrosine/3,4-dihydroxyphenylalanine decarboxylase gene family Plant Physiol 110 43-9.

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

 Hiruma, K.; Carter, M. S.; Riddiford, L. M. (1995) Characterization of the dopa decarboxylase gene of Manduca sexta and its suppression by 20-hydroxyecdysone Dev Biol 169 195-209.

 Kawalleck, P.; Keller, H.; Hahlbrock, K.; Scheel, D.; Somssich, I.E. (1993) A pathogen-responsive gene of parsley encodes tyrosine decarboxylase J Biol Chem 268 2189-94.

 Park, D. H.; Kim, K. T.; Choi, M. U.; Samanta, H.; Joh, T. H. (1992) Characterization of bovine aromatic L-amino acid decarboxylase expressed in a mouse cell line: comparison with native enzyme Brain Res Mol Brain Res 16 232-8.

 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 2582-6.

 Ichinose, H.; Kurosawa, Y.; Titani, K.; Fujita, K.; Nagatsu, T. (1989) Isolation and characterization of a cDNA clone encoding human aromatic L-amino acid decarboxylase Biochem Biophys Res Commun 164 1024-30.

Articles on 4.1.1.28
 
last changed 2014/03/20 11:57

B6db activities