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DDC  -  dopa decarboxylase (aromatic L-amino acid...

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Disease relevance of DDC


High impact information on DDC

  • DOPA decarboxylase (DDC) is responsible for the synthesis of the key neurotransmitters dopamine and serotonin via decarboxylation of L-3,4-dihydroxyphenylalanine (L-DOPA) and L-5-hydroxytryptophan, respectively [1].
  • Another 50% of the nerve cell bodies contained immunoreactivity (IR) to dopamine-beta-hydroxylase (DBH), but did not have any other characteristics of noradrenergic neurons; they did not contain detectable catecholamines, or IR to dopa decarboxylase (DDC) or tyrosine (TH) hydroxylase, nor did they take up exogenous catecholamines [4].
  • Concurrent with this reaction, 5-HT inactivates DDC in both a time- and concentration-dependent manner and exhibits saturation of the rate of inactivation at high concentrations, with Ki and Kinact values of 0.40 mM and 0.023 min-1, respectively [2].
  • Taken together, these findings indicate that recombinant pig kidney DDC has two active-site PLP molecules and therefore displays structural characteristics typical of PLP-dependent homodimeric enzymes [5].
  • All these data, besides validating the functional DDC active site model, represent an important step toward the elucidation of the catalytic pathway of oxidative deamination [6].

Biological context of DDC


Anatomical context of DDC

  • Contrary to expectation, co-grafting of transfected GDNF-expressing HiB5 cells, a rat-derived neural cell line, tended to impair the survival of the grafts with the lowest values for graft volumes, TH-positive cell numbers, behavioral scores, and relative DOPA decarboxylase activity [11].

Associations of DDC with chemical compounds


Analytical, diagnostic and therapeutic context of DDC


  1. Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase. Burkhard, P., Dominici, P., Borri-Voltattorni, C., Jansonius, J.N., Malashkevich, V.N. Nat. Struct. Biol. (2001) [Pubmed]
  2. Mechanism-based inactivation of dopa decarboxylase by serotonin. Bertoldi, M., Moore, P.S., Maras, B., Dominici, P., Voltattorni, C.B. J. Biol. Chem. (1996) [Pubmed]
  3. Characterization of DOPA decarboxylase mRNA in rat pheochromocytoma. Bruneau, G., Krieger-Poullet, M., Coge, F., Borri-Voltattorni, C., Gros, F., Thibault, J. Biochimie (1990) [Pubmed]
  4. Neuronal colocalization of peptides, catecholamines, and catecholamine-synthesizing enzymes in guinea pig paracervical ganglia. Morris, J.L., Gibbins, I.L. J. Neurosci. (1987) [Pubmed]
  5. Cloning and expression of pig kidney dopa decarboxylase: comparison of the naturally occurring and recombinant enzymes. Moore, P.S., Dominici, P., Borri Voltattorni, C. Biochem. J. (1996) [Pubmed]
  6. A quinonoid is an intermediate of oxidative deamination reaction catalyzed by Dopa decarboxylase. Bertoldi, M., Cellini, B., Maras, B., Voltattorni, C.B. FEBS Lett. (2005) [Pubmed]
  7. Reaction and substrate specificity of recombinant pig kidney Dopa decarboxylase under aerobic and anaerobic conditions. Bertoldi, M., Borri Voltattorni, C. Biochim. Biophys. Acta (2003) [Pubmed]
  8. Substrate stereospecificity and selectivity of catechol-O-methyltransferase for DOPA, DOPA derivatives and alpha-substituted catecholamines. Gordonsmith, R.H., Raxworthy, M.J., Gulliver, P.A. Biochem. Pharmacol. (1982) [Pubmed]
  9. Acute neuroleptic stimulates DOPA decarboxylase in porcine brain in vivo. Danielsen, E.H., Smith, D., Hermansen, F., Gjedde, A., Cumming, P. Synapse (2001) [Pubmed]
  10. A rapid assay for tyrosine hydroxylase activity, an indicator of chronic stress in laboratory and domestic animals. Chobotská, K., Arnold, M., Werner, P., Pliska, V. Biol. Chem. (1998) [Pubmed]
  11. Quantitative [18F]fluorodopa/PET and histology of fetal mesencephalic dopaminergic grafts to the striatum of MPTP-poisoned minipigs. Dall, A.M., Danielsen, E.H., Sørensen, J.C., Andersen, F., Møller, A., Zimmer, J., Gjedde, A.H., Cumming, P. Cell transplantation. (2002) [Pubmed]
  12. Mutation of cysteine 111 in Dopa decarboxylase leads to active site perturbation. Dominici, P., Moore, P.S., Castellani, S., Bertoldi, M., Voltattorni, C.B. Protein Sci. (1997) [Pubmed]
  13. Green tea polyphenols: novel irreversible inhibitors of dopa decarboxylase. Bertoldi, M., Gonsalvi, M., Voltattorni, C.B. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  14. Crystallization and preliminary X-ray analysis of pig kidney DOPA decarboxylase. Malashkevich, V.N., Filipponi, P., Sauder, U., Dominici, P., Jansonius, J.N., Borri Voltattorni, C. J. Mol. Biol. (1992) [Pubmed]
  15. Involvement of catecholamines in Haemophilus influenzae induced decrease of beta-adrenoceptor function. Schreurs, A.J., Versteeg, D.H., Nijkamp, F.P. Naunyn Schmiedebergs Arch. Pharmacol. (1982) [Pubmed]
  16. Transaldimination induces coenzyme reorientation in pig kidney dopa decarboxylase. Moore, P.S., Dominici, P., Voltattorni, C.B. Biochimie (1995) [Pubmed]
  17. Some aspects on L-dopa decarboxylase and p-tyrosine decarboxylase in the central nervous and peripheral tissues of the American cockroach Periplaneta americana. Yu, P.H., Sloley, B.D. Comp. Biochem. Physiol. C, Comp. Pharmacol. Toxicol. (1987) [Pubmed]
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