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(2S)-2-amino-3-(3-hydroxyphenyl)-2-methylpropanoic acid
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(2S)-2-amino-3-(4-hydroxyphenyl)-2-methylpropanoic acid
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(S)-alpha-(fluoromethyl)tryptophan
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the suicide substrate effectively inhibits TDC activity extracted from rice leaves infected by Bipolaris oryzae and the inhibition rate increases dependent on preincubation time
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
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MPTP, after 7 days of treatment, AAAD activities are decreased by more than 50% in the mouse striatum
2,3,4-Trihydroxybenzylhydrazine
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2-Phenylethylamine
Micrococcus percitreus
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competitive inhibition, 80% inhibition at 0.5 mM
2-[1-[4-hydroxy-5-[3-(3-hydroxy-4-methoxyphenyl)propyl]-2-methoxyphenyl]-3-(4-hydroxy-3-methoxyphenyl)propyl]-5-methoxycyclohexa-2,5-diene-1,4-dione
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inhibitor isolated from Euonymus glabra Roxb.
2-[[(2-oxo-2,3-dihydro-1H-benzimidazol-5-yl)sulfonyl]amino]-N-phenylbenzamide
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competitive. Inhibitor is unable to bind free pyridoxal 5'-phosphate, and predicted to not cross the blood-brain barrier
3'-hydroxybenzylhydrazine
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NSD-1015, a central aromatic L-amino acid decarboxylase inhibitor
3,4-dihydroxyphenylalanine
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inhibitory effect of 3,4-dihydroxyphenylalanine on the conversion of 5-hydroxy-L-tryptophan
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.
3-hydroxy-benzylhydrazine
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3-[2-hydroxy-5-[3-(4-hydroxy-3-methoxyphenyl)propyl]-4-methoxyphenyl]-2-[3-(4-hydroxy-3-methoxyphenyl)-2-oxopropyl]-5-methoxycyclohexa-2,5-diene-1,4-dione
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inhibitor isolated from Euonymus glabra Roxb., structural analogue of dopamine. Compound is able to suppress the activity of dopa decarboxylase and dopamine levels in purified enzyme and cell-based assays
4-Bromo-3-hydroxy-benzyloxyamine
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4-[(E)-[(3-phenyl-5-sulfanyl-4H-1,2,4-triazol-4-yl)imino]methyl]benzene-1,2,3-triol
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mixed type inhibition. Inhibitor is unable to bind free pyridoxal 5'-phosphate, and predicted to not cross the blood-brain barrier
4-[(E)-[(3-phenyl-5-sulfanyl-4H-1,2,4-triazol-4-yl)imino]methyl]benzene-1,2-diol
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competitive. Inhibitor is unable to bind free pyridoxal 5'-phosphate, and predicted to not cross the blood-brain barrier
4-[(E)-[[3-(4-chlorophenyl)-5-sulfanyl-4H-1,2,4-triazol-4-yl]imino]methyl]benzene-1,2-diol
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competitive. Inhibitor is unable to bind free pyridoxal 5'-phosphate, and predicted to not cross the blood-brain barrier
5-hydroxy indole acetic acid
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the conversion of 5-hydroxy-L-tryptophan is 20% inhibited by 0.33 mM 5-hydroxy indole acetic acid
7-hydroxy-N,N-di-n-propyl-2-aminotetralin
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reduced AAAD activity in the striatum by acute treatment with the D2-like receptor agonist
alpha-methyl-2,4-dihydroxyphenylalanine
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alpha-Methyl-5-hydroxytryptophan
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alpha-Methyl-D,L-3,4-dihydroxyphenylalanine
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alpha-methyl-DL-phenylalanine
alpha-methyl-DL-tyrosine
Micrococcus percitreus
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71% inhibition at 0.2 mM
alpha-methyl-L-Dopa
Micrococcus percitreus
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60% inhibition at 0.2 mM
alpha-Methylhydrazinodopa
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alpha-monofluoromethyl-DL-3,4-dihydroxyphenylalanine
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suicide inhibitor
alpha-synuclein
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significantly reduces AADC activity
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annexin 5
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endogenous inhibitor, identified and purified from human placenta presented in the membrane function, shows 30.4% inhibition by incubation of the human placenta samples in the presence of 0.34 unit ddc from mouse kidney homogenate. The inhibitor exhibits an optimum activity at 50 mM NaCl, pH 6.5, is heat labile and is deactivated by boiling. After incubation of the placental homogenate with proteinase K, inhibitory activity is partially abolished, suggesting that a population of inhibitor molecules is embedded in the membrane.
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apomorphine
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inhibition in rat striatum
benzerazide
Escherichia coli phagocytosis is blocked by benzerazide, revealing the involvement of Ddc activity in phagocytosis
beta-phenylethylamine
Micrococcus percitreus
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bromocryptine
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reduced AAAD activity in the striatum by acute and chronic treatment with the D2-like receptor agonist
Chalcone derivatives
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Clorgyline
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reduced AAAD activity in the striatum by acute treatment with the dopamine receptor indirect agonist
D-5-hydroxytryptophan
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D-tryptophan
non-competitive inhibitor
diethyldithiocarbamate
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Dithiobisnitrobenzoate
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DL-alpha-Difluoromethyl-beta-(3,4-dihydroxyphenyl)alanine
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DL-alpha-Monofluoromethyl-beta-(3,4-dihydroxyphenyl)alanine
DL-m-Tyr
Micrococcus percitreus
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tryptamine formation
DL-m-tyrosine
Micrococcus percitreus
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50% inhibition at 4 mM
epigallocatechin-3-gallate
Fe2+
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enzyme from pharate pupae, no effect on the enzyme from white prepupae
Fluoromethyl dopamine
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histamine
Micrococcus percitreus
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1% inhibition at 4 mM
L-3,4-dihydroxyphenylalanine
Micrococcus percitreus
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tryptamine formation
L-alpha-Methyl-alpha-hydrazino-3,4-dihydroxyphenylpropionic acid
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L-histidine
Micrococcus percitreus
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5% inhibition at 4 mM
L-Phe
Micrococcus percitreus
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tryptamine formation
L-phenylalanine
Micrococcus percitreus
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uncompetitive inhibition, 53% inhibition at 0.5 mM
L-Tyr
Micrococcus percitreus
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tryptamine formation
L-tyrosine
Micrococcus percitreus
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uncompetitive inhibition, 38% inhibition at 0.5 mM
N,N-Dimethyltryptamine
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N-5'-Phosphopyridoxyl-L-dopa
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N1-Seryl N2-(2,3,4-trihydroxybenzyl) hydrazine
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p-chloromercuribenzoic acid
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Pargyline
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reduced AAAD activity in the striatum by acute treatment with the dopamine receptor indirect agonist
potassium bicarbonate
Micrococcus percitreus
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57% inhibition at 1 M
pyridoxamine phosphate
Micrococcus percitreus
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complete inhibition at 0.2 mM
quinpirole
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reduced AAAD activity in the striatum by chronic treatment with the D2-like receptor agonist
R-(+)-Amino-4,5-dihydroxy-1,2-7,8-tetrahydronaphthalene
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testosterone propionate
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repetitive treatment of female mice with testosterone propionate for 2 weeks elicits a marked decrease in renal DCC activity
3-Indoleacetamide
Micrococcus percitreus
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3-Indoleacetamide
Micrococcus percitreus
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27% inhibition at 0.25 mM
3-Indolealdehyde
Micrococcus percitreus
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3-Indolealdehyde
Micrococcus percitreus
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33% inhibition at 0.25 mM
5-hydroxy-L-tryptophan
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strong inhibitory effect of 5-hydroxy-L-tryptophan on the conversion of 3,4-dihydroxyphenylalanine
5-hydroxy-L-tryptophan
substrate inhibition
5-hydroxytryptophan
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Al3+
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Al3+
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enzyme from pharate pupae, no effect on the enzyme from white prepupae
alpha-methyl-DL-phenylalanine
Micrococcus percitreus
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76% inhibition at 0.2 mM
alpha-methyl-DL-phenylalanine
Micrococcus percitreus
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competitive inhibition
Amb2470350
a reversible competitive inhibitor
Amb2470350
a reversible competitive inhibitor
Amb2470350
a reversible competitive inhibitor
Benserazide
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Benserazide
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competitive inhibitor of L-Dopa, but a non-competitive inhibitor of 5-hydroxytryptophan
Benserazide
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levels of intracellular dopamine after L-DOPA treatment (0.02 and 0.1 mM) are significantly decreased by the AADC inhibitor benserazide (0.02 mM) for 6-24 h exposure prior to L-DOPA treatment in PC12 cells, the 230%-350% increases in dopamine levels by L-DOPA are reduced to 187%-284% by benserazide for 6 h
Benserazide
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peripheral inhibitor
Benserazide
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intrastriatal inhibition of the enzyme prevents the appearance of L-dopa-induced dyskinetic movements at the lesioned side
BH4
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carbidopa
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carbidopa
Escherichia coli phagocytosis is blocked by carbidopa, revealing the involvement of Ddc activity in phagocytosis
carbidopa
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strongly inhibited by increasing concentrations of carbidopa, at a concentration of 0.4 mM carbidopa the conversion of 3,4-dihydroxyphenylalanine is completely inhibited, at a concentration of 0.25 mM the conversion of 5-hydroxy-L-tryptophan is completely inhibited
carbidopa
Thr82 is implicated in 4'-hydroxyl catechol ring binding
carbidopa
the compound is able to block the reaction at the Michaelis complex step in DDC
carbidopa
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non-competitive inhibitor
carbidopa
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levels of intracellular dopamine after L-DOPA treatment (0.02 and 0.1 mM) are significantly decreased by the AADC inhibitor carbidopa (0.020 mM) for 6-24 h exposure prior to L-DOPA treatment in PC12 cells, the 230%-350% increases in dopamine levels by L-DOPA are reduced to 187%-284% by 153%-248% by carbidopa for 6 h
Cu2+
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Cu2+
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enzyme from pharate pupae, no effect on the enzyme from white prepupae
DL-alpha-Monofluoromethyl-beta-(3,4-dihydroxyphenyl)alanine
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DL-alpha-Monofluoromethyl-beta-(3,4-dihydroxyphenyl)alanine
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DL-alpha-Monofluoromethyl-beta-(3,4-dihydroxyphenyl)alanine
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DL-alpha-Monofluoromethyl-beta-(3,4-dihydroxyphenyl)alanine
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dopamine
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the conversion of 5-hydroxy-L-tryptophan is strongly inhibited by dopamine
dopamine
Micrococcus percitreus
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dopamine
Micrococcus percitreus
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complete inhibition at 0.5 mM
epigallocatechin-3-gallate
EGCG, the inhibitory effect is mediated by blocking the entrance to the catalytic site, therefore, preventing substrate binding
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
epinephrine
Micrococcus percitreus
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epinephrine
Micrococcus percitreus
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30% inhibition at 4 mM
Hg2+
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Hg2+
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enzyme from pharate pupae, no effect on the enzyme from white prepupae
hydroxylamine
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L-Dopa
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20.3% decrease in activity in corpus striatum following a 2 years treatment
L-Dopa
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slight substrate inhibition is observed at high concentration of L-Dopa
L-Dopa
Micrococcus percitreus
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competitive inhibition, 98% inhibition at 1 mM
L-Dopa
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reduced AAAD activity in the striatum by acute and chronic treatment with the dopamine receptor indirect agonist
L-Dopa
substrate inhibition
Methyldopa
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alpha-methyldopa
N-acetyldopamine
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NEM
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NEM
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1 mM, complete inhibition
norepinephrine
Micrococcus percitreus
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norepinephrine
Micrococcus percitreus
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40% inhibition at 4 mM
NSD-1015
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NSD-1015
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non-competitive inhibitor
PCMB
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pyridoxal 5'-phosphate
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inhibition at high concentrations, stimulation at lower concentration
pyridoxal 5'-phosphate
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optimal concentration for pharate pupae enzyme: 0.02 mM; optimal concentration for the white pupae enzyme: 0.4 mM
Semicarbazide
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serotonin
and/or its aldehyde, behaves as a mechanism-based inhibitor, product inhibition
serotonin
Micrococcus percitreus
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2% inhibition at 4 mM
serotonin
and/or its aldehyde, behaves as a mechanism-based inhibitor, product inhibition
serotonin
and/or its aldehyde, behaves as a mechanism-based inhibitor, product inhibition
tryptamine
competitive inhibitor
tryptamine
Micrococcus percitreus
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5% inhibition at 1 mM
tyramine
Micrococcus percitreus
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tyramine
Micrococcus percitreus
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competitive inhibition, 71% inhibition at 0.5 mM
Zn2+
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Zn2+
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enzyme from pharate pupae,no effect on the enzyme from white prepupae
additional information
decrease of Escherichia coli phagocytosis in the presence of Ddc small interfering RNA of about 30%, compared with the controls; Escherichia coli phagocytosis is blocked by small interfering RNA for Ddc and antibodies against Ddc, revealing the involvement of Ddc activity in phagocytosis. Haemocyte-surface-associated Ddc is decreased by about 90% in haemocytes transfected with Ddc siRNA, compared to the control experiment; when haemocytes are pretreated with anti-Ddc instead of Ddc small interfering RNA before challenge with Escherichia coli, a greater decrease of Escherichia coli phagocytosis (about 60%) is observed, compared with the siRNA results (30%)
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additional information
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decrease of Escherichia coli phagocytosis in the presence of Ddc small interfering RNA of about 30%, compared with the controls; Escherichia coli phagocytosis is blocked by small interfering RNA for Ddc and antibodies against Ddc, revealing the involvement of Ddc activity in phagocytosis. Haemocyte-surface-associated Ddc is decreased by about 90% in haemocytes transfected with Ddc siRNA, compared to the control experiment; when haemocytes are pretreated with anti-Ddc instead of Ddc small interfering RNA before challenge with Escherichia coli, a greater decrease of Escherichia coli phagocytosis (about 60%) is observed, compared with the siRNA results (30%)
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additional information
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not sensitive to diisopropyl flurophosphate
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additional information
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not inhibited by 3-methoxy-tyrosine, homovanillic acid, or 5-hydroxy-tryptamine
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additional information
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diminished AAAD activity in dopaminergic cells that overexpress alpha-sinuclein
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additional information
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increasing concentrations of the serine protease inhibitor aprotinin have a minimal inhibitory effect on enzyme solubilization while leupeptin inhibits release of membrane-bound enzyme
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additional information
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4-benzoquinone might be the crucial chemical moiety for binding and inhibiting human DOPA decarboxylase
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additional information
the inhibitory principle is based on a hydrazine group that forms a hydrazone derivative with pyridoxal 5'-phosphate, thus blocking it and inactivating the enzyme. Thus, a greater amount of L-Dopa can reach the brain where it can be transformed to dopamine ameliorating disease symptoms. Compounds acting via a suicide mechanism by alkylating the enzyme: alpha-chloromethyl and alpha-fluoromethyl derivatives of Dopa, alpha-vinyl-Dopa 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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additional information
successful strategies to inhibit the decarboxylase have included the synthesis of fluoro-derivatives, which act as competitive and/or suicide inhibitors, as it is the case of several fluoro-dopa derivatives
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additional information
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successful strategies to inhibit the decarboxylase have included the synthesis of fluoro-derivatives, which act as competitive and/or suicide inhibitors, as it is the case of several fluoro-dopa derivatives
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additional information
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overview
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additional information
Micrococcus percitreus
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not inhibited by D-tryptophan, kynuramine, octopamine, and 3-indoleacetate
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additional information
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in castrated male mice, DCC activity decreases in all parts of the small intestine, reaching values similar to those in females
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additional information
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not inhibited by L-alpha-fluoromethyltyrosine and L-alpha-fluoromethyl(3,4-dihydroxyphenyl)alanine
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additional information
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human autoantibody
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additional information
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dopamine receptor activation decreases AAAD activity
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additional information
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L-3,4-dihydroxyphenylalanine (100 mg/kg) increases the striatal dopamine content but elicits no effect on locomotor activity in the presence of benserazide (50 mg/kg i.p.), a peripheral AADC inhibitor. L-3,4-dihydroxyphenylalanine increases the dopamine content in the presence of 3'-hydroxybenzylhydrazine to a maximal degree similar to that in the presence of benserazide. L-3,4-dihydroxyphenylalanine cyclohexyl ester is a suitable L-3,4-dihydroxyphenylalanine antagonist that would be available under in vivo experimental conditions.; L-3,4-dihydroxyphenylalanine cyclohexyl ester would antagonize the behavioral responses of conscious rats to L-3,4-dihydroxyphenylalanine in the presence of 3'-hydroxybenzylhydrazine. L-3,4-dihydroxyphenylalanine cyclohexyl ester elicits a dose-dependent partial antagonism against the increase in locomotor activity induced by L-3,4-dihydroxyphenylalanine. A low dose of L-3,4-dihydroxyphenylalanine cyclohexyl ester (10 mg/kg) elicits full antagonism against the potentiating effect of a non-effective dose of L-3,4-dihydroxyphenylalanine (20 mg/kg) on the increase in locomotor activity induced by a dopamine D2 agonist quinpirole (0.3 mg/kg s.c.). L-3,4-dihydroxyphenylalanine cyclohexyl ester elicits full antagonism against licking behavior induced by L-3,4-dihydroxyphenylalanine.
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additional information
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a decrease in urinary levels of dopamine and in renal AADC activity at 20 twenty-six weeks after renal mass ablation
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additional information
compounds acting via a suicide mechanism by alkylating the enzyme: alpha-chloromethyl and alpha-fluoromethyl derivatives of Dopa, alpha-vinyl-Dopa 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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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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