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5-hydroxy-L-tryptophan
5-hydroxytryptamine + CO2
-
-
-
?
5-hydroxy-L-tryptophan
serotonin + CO2
-
-
-
?
L-phenylalanine
phenylethylamine + CO2
-
-
-
ir
L-Trp
Tryptamine + CO2
-
-
-
ir
2-fluoro-DOPA
?
-
-
-
-
?
2-fluoro-L-(3,4-dihydroxyphenyl)alanine
4-(2-aminoethyl)-3-fluorobenzene-1,2-diol + CO2
-
-
-
?
3,4-Dihydroxyphenylalanine
3-Hydroxytyramine + CO2
-
-
-
-
?
5-fluoro-DOPA
?
-
-
-
-
?
5-fluoro-L-(3,4-dihydroxyphenyl)alanine
5-(2-aminoethyl)-3-fluorobenzene-1,2-diol + CO2
-
-
-
?
5-hydroxy-L-tryptophan
5-hydroxytryptamine + CO2
-
-
-
-
?
5-hydroxy-L-tryptophan
serotonin + CO2
-
-
-
?
5-hydroxytryptamine + O2
5-hydroxyindolacetaldehyde + NH3
-
side reaction, decarboxylation-dependent transamination
-
?
5-Hydroxytryptophan
Serotonin + CO2
-
-
-
-
?
6-fluoro-DOPA
?
-
-
-
-
?
6-fluoro-L-(3,4-dihydroxyphenyl)alanine
4-(2-aminoethyl)-5-fluorobenzene-1,2-diol + CO2
-
-
-
?
6-fluoro-threo-(3,4-dihydroxyphenyl)serine
4-(2-aminoethyl)-5-fluorobenzene-1,2-diol + CO2
-
-
-
?
alpha-methyl-dopamine + O2
3,4-dihydroxyphenylacetone + NH3
-
side reaction, decarboxylation-dependent transamination
-
?
alpha-methyl-L-Dopa
alpha-methyl-dopamine + CO2
dopamine + O2
3,4-dihydroxyphenylacetaldehyde + NH3
-
-
-
?
L-(3,4-dihydroxyphenyl)alanine
4-(2-aminoethyl)benzene-1,2-diol + CO2
-
-
-
?
L-5-hydroxytryptophan
5-hydroxytryptamine + CO2
-
-
-
?
L-threo-(3,4-dihydroxyphenyl)serine
4-[(2-hydroxyethyl)amino]benzene-1,2-diol + CO2
-
-
-
?
L-Trp
Tryptamine + CO2
-
-
-
-
?
L-tryptophan
tryptamine + CO2
additional information
?
-
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
ir
alpha-methyl-L-Dopa
alpha-methyl-dopamine + CO2
-
-
-
?
alpha-methyl-L-Dopa
alpha-methyl-dopamine + CO2
-
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
-
?
L-tryptophan
tryptamine + CO2
-
-
-
?
L-tryptophan
tryptamine + CO2
-
-
-
?
L-tryptophan
tryptamine + CO2
-
-
-
?
L-tryptophan
tryptamine + CO2
-
-
-
?
additional information
?
-
the pig DDC is able to catalyze oxidative deamination of aromatic amines, cf. EC 4.3.1., and the generated carbonyl compounds act as suicide or mechanism-based inhibitors of the enzyme, catalytic mechanism with formation of a ketimine and superoxide as reaction intermediates, overview. The stoichiometry of dioxygen consumed with respect to carbonyl compound and ammonia formed as well as amine oxidized is 1:2. Studies with an analogue of serotonin undergoing oxidative deamination with DDC, i.e. D-tryptophan methyl ester, shows the accumulation of the quinonoid intermediate of this reaction
-
-
?
additional information
?
-
-
exhibits half-transaminase activity toward D-aromatic amino acids and oxidative deaminase activity toward aromatic amines
-
?
additional information
?
-
-
catalyzes the decarboxylation of aromatic amino acids into their corresponding amines
-
-
?
additional information
?
-
-
the enzyme is responsible for the decarboxylation step in both the catecholamine and the indolamine synthetic pathways. The enzyme is regulated by a short term mechanism that may involve activation of adenyl cyclase or protein kinase C
-
-
?
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3-(3,4-dihydroxyphenyl)-2-hydrazino-2-methyl propionic acid
carbiDOPA, addition of 10 microM inhibitor to reaction mixtures (Y332F mutant with L-dopa) in the presence or in the absence of catalase or superoxide dismutase, immediately stops the O2 consumption.
5-hydroxy-L-tryptophan
substrate inhibition
Amb2470350
a reversible competitive inhibitor
epigallocatechin-3-gallate
direct inhibitory effect on both histidine decarboxylase and DOPA decarboxylase. Modeling of binding to the enzymes. Epigallocatechin-3-gallate does not affect the quaternary structure of the enzyme and remains stable in the active site throughout the entire trajectory. After 700 ps of simulation, epigallocatechin-3-gallate moves deeper into the active site. While adopting this conformation, epigallocatechin-3-gallate actually fills the binding pocket and blocks its entrance pathway
L-Dopa
substrate inhibition
serotonin
and/or its aldehyde, behaves as a mechanism-based inhibitor, product inhibition
2,3,4-Trihydroxybenzylhydrazine
-
-
Dithiobisnitrobenzoate
-
-
DL-alpha-Difluoromethyl-beta-(3,4-dihydroxyphenyl)alanine
-
-
DL-alpha-Monofluoromethyl-beta-(3,4-dihydroxyphenyl)alanine
-
-
L-alpha-Methyl-alpha-hydrazino-3,4-dihydroxyphenylpropionic acid
-
-
additional information
compounds acting via a suicide mechanism by alkylating the enzyme: alpha-chloromethyl and alpha-fluoromethyl derivatives of Dopa, a-vinylDopa and alpha-acetylenic Dopa. The phosphopyridoxyl aromatic amino acids Schiff base analogues and substrate analogues, like green tea polyphenols, also inhibit the enzyme
-
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Christenson, J.G.; Dairman, W.; Udenfrien, S.
On the identity of DOPA decarboxylase and 5-hydroxytryptophan decarboxylase
Proc. Natl. Acad. Sci. USA
69
343-347
1972
Oryctolagus cuniculus, Rattus norvegicus, Sus scrofa
brenda
Minelli, A.; Charteris, A.T.; Voltattorni, C.B.; John, R.A.
Reactions of DOPA (3,4-dihydroxyphenylalanine) decarboxylase with DOPA
Biochem. J.
183
361-368
1979
Sus scrofa
brenda
Groen, B.W.; van der Meer, R.A.; Duine, J.A.
Evidence for PQQ as cofactor in 3,4-dihydroxyphenylalanine (dopa) decarboxylase of pig kidney
FEBS Lett.
237
98-102
1988
Sus scrofa
brenda
Voltattorni, C.B.; Minelli, A.; Vecchini, P.; Fiori, A.; Turano, C.
Purification and characterization of 3,4-dihydroxyphenylalanine decarboxylase from pig kidney
Eur. J. Biochem.
93
181-188
1979
Sus scrofa
brenda
Voltattorni, C.B.; Giartosio, A.; Turano, C.
Aromatic-L-amino acid decarboxylase from pig kidney
Methods Enzymol.
142
179-187
1987
Sus scrofa
brenda
Zhu, M.Y.; Juorio, A.V.
Aromatic L-amino acid decarboxylase: biological characterization and functional role
Gen. Pharmacol.
26
681-696
1995
Bos taurus, Cavia porcellus, Homo sapiens, Rattus norvegicus, Sus scrofa, Xenopus laevis
brenda
Dominici, P.; Moore, P.S.; Voltattorni, C.B.
Modified purification of L-aromatic amino acid decarboxylase from pig kidney
Protein Expr. Purif.
4
345-347
1993
Sus scrofa
brenda
Borresen, T.; Klausen, N.K.; Larsen, L.; Sorensen, H.
Purification and characterization of tyrosine decarboxylase and aromatic-L-amino-acid decarboxylase
Biochim. Biophys. Acta
993
108-115
1989
Sus scrofa
brenda
Tancini, B.; Dominici, P.; Simmaco, M.; Schinina, M.E.; Barra, D.; Voltattorini, C.B.
Limited tryptic proteolysis of pig kidney 3,4-dihydroxyphenylalanine decarboxylase
Arch. Biochem. Biophys.
260
569-576
1988
Sus scrofa
brenda
Borri Voltattorni, C.; Bertoldi, M.; Bianconi, S.; Deng, W.p.; Wong, K.; Kim, I.; Herbert, B.; Kirk, K.L.
Behavior of fluorinated analogs of L-(3,4-dihydroxyphenyl)alanine and L-threo-(3,4-dihydroxyphenyl)serine as substrates for Dopa decarboxylase
Biochem. Biophys. Res. Commun.
295
107-111
2002
Sus scrofa
brenda
Bertoldi, M.; Borri Voltattorni, C.
Reaction of dopa decarboxylase with L-aromatic amino acids under aerobic and anaerobic conditions
Biochem. J.
352
533-538
2000
Sus scrofa
-
brenda
Bertoldi, M.; Borri Voltattorni, C.
Reaction and substrate specificity of recombinant pig kidney DOPA decarboxylase under aerobic and anaerobic conditions
Biochim. Biophys. Acta
1647
42-47
2003
Sus scrofa
brenda
Facchini, P.J.; Huber-Allanach, K.L.; Tari, L.W.
Plant aromatic L-amino acid decarboxylases: evolution, biochemistry, regulation, and metabolic engineering applications
Phytochemistry
54
121-138
2000
Cinchona calisaya, Drosophila melanogaster, Solanum lycopersicum, Sus scrofa, Cinchona officinalis, Catharanthus roseus (P17770), Homo sapiens (P20711), Camptotheca acuminata (P93082)
brenda
Brust, P.; Walter, B.; Hinz, R.; Fuchtner, F.; Muller, M.; Steinbach, J.; Bauer, R.
Developmental changes in the activities of aromatic amino acid decarboxylase and catechol-O-methyl transferase in the porcine brain: a positron emission tomography study
Neurosci. Lett.
364
159-163
2004
Sus scrofa
brenda
Bertoldi, M.; Cellini, B.; Montioli, R.; Borri Voltattorni, C.
Insights into the mechanism of oxidative deamination catalyzed by DOPA decarboxylase
Biochemistry
47
7187-7195
2008
Sus scrofa (P80041)
brenda
Lin, Y.L.; Gao, J.
Internal proton transfer in the external pyridoxal 5'-phosphate Schiff base in dopa decarboxylase
Biochemistry
49
84-94
2010
Sus scrofa (P80041)
brenda
Blechingberg, J.; Holm, I.E.; Johansen, M.G.; B?rglum, A.D.; Nielsen, A.L.
Aromatic L-amino acid decarboxylase expression profiling and isoform detection in the developing porcine brain
Brain Res.
1308
1-13
2010
Sus scrofa
brenda
Lin, Y.L.; Gao, J.
Kinetic isotope effects of L-Dopa decarboxylase
J. Am. Chem. Soc.
133
4398-4403
2011
Sus scrofa
brenda
Chakrabarty, K.; Gupta, S.N.; Das, G.K.; Roy, S.
Theoretical studies on the pyridoxal-5-phosphate dependent enzyme dopa decarboxylase: effect of Thr 246 residue on the co-factor-enzyme binding and reaction mechanism
Indian J. Biochem. Biophys.
49
155-164
2012
Sus scrofa (P80041)
brenda
Ruiz-Perez, M.V.; Pino-Angeles, A.; Medina, M.A.; Sanchez-Jimenez, F.; Moya-Garcia, A.A.
Structural perspective on the direct inhibition mechanism of EGCG on mammalian histidine decarboxylase and DOPA decarboxylase
J. Chem. Inf. Model.
52
113-119
2012
Sus scrofa (P80041)
brenda
Barboni, E.; Borri Voltattorni, C.; DErme, M.; Fiori, A.; Minelli, A.; Rosei, M.; Turano, C.
An abnormal reaction occurring in the presence of L-aromatic aminoacid decarboxylase
Biochem. Biophys. Res. Commun.
99
576-583
1981
Sus scrofa
brenda
Bertoldi, M.
Mammalian dopa decarboxylase structure, catalytic activity and inhibition
Arch. Biochem. Biophys.
546
1-7
2014
Rattus norvegicus (P14173), Homo sapiens (P20711), Sus scrofa (P80041)
brenda