Any feedback?
Information on EC 4.1.1.28 - aromatic-L-amino-acid decarboxylase and Organism(s) Rattus norvegicus and UniProt Accession P14173
for references in articles please use BRENDA:EC4.1.1.28Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.1.1.28 aromatic-L-amino-acid decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein. The enzyme also acts on some other aromatic L-amino acids, including L-tryptophan, L-tyrosine and L-phenylalanine.
Specify your search results
Word Map
- 4.1.1.28
-
dopaminergic
- serotonin
- parkinsonism
-
monoamine
- striatum
- catecholamine
-
neurotransmitter
- carbidopa
- noradrenaline
- levodopa
- norepinephrine
- benserazide
- 5-hydroxytryptamine
-
substantia
-
dopac
-
serotonergic
- tryptamine
-
nigrostriatal
- catharanthus
- catechol-o-methyltransferase
- roseus
- beta-hydroxylase
-
5-hydroxyindoleacetic
-
homovanillic
-
3,4-dihydroxyphenylacetic
-
catecholaminergic
- dyskinesia
- dopamine-beta-hydroxylase
- alpha-methyl-p-tyrosine
-
5-hiaa
- pargyline
- strictosidine
-
monoaminergic
-
raphe
-
l-dopa-induced
- l-dihydroxyphenylalanine
- apomorphine
-
antiparkinsonian
- gamma-butyrolactone
-
tuberoinfundibular
-
autoreceptors
- 3-methoxytyramine
- quinpirole
- entacapone
-
catecholamine-synthesizing
-
dihydroxyphenylacetic
-
non-dopaminergic
- phenylethanolamine
- pharmacology
- analysis
-
6-hydroxydopamine-lesioned
- medicine
- drug development
- synthesis
- tolcapone
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dopa decarboxylase, aromatic l-amino acid decarboxylase, aromatic amino acid decarboxylase, tryptophan decarboxylase, l-dopa decarboxylase, l-aromatic amino acid decarboxylase, aromatic-l-amino-acid decarboxylase, l-amino-acid decarboxylase, 3,4-dihydroxyphenylalanine decarboxylase, dopamine decarboxylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3,4-Dihydroxyphenylalanine decarboxylase
-
-
-
-
5-Hydroxy-L-tryptophan decarboxylase
-
-
-
-
5-Hydroxytryptophan decarboxylase
-
-
-
-
AADC
Aromatic amino acid decarboxylase
Aromatic L-amino acid decarboxylase
DDC
-
-
-
-
Decarboxylase, aromatic amino acid
-
-
-
-
Dihydroxyphenylalanine-5-hydroxytryptophan decarboxylase
-
-
-
-
DOPA DC
-
-
-
-
DOPA decarboxylase
DOPA-5-hydroxytryptophan decarboxylase
-
-
-
-
Hydroxytryptophan decarboxylase
-
-
-
-
L-3,4-Dihydroxyphenylalanine decarboxylase
-
-
-
-
L-5-Hydroxytryptophan decarboxylase
-
-
-
-
L-Aromatic amino acid decarboxylase
-
-
-
-
L-DOPA decarboxylase
-
-
-
-
L-Tryptophan decarboxylase
-
-
-
-
Tryptophan decarboxylase
TYDC
-
-
-
-
Tyrosine/Dopa decarboxylase
-
-
-
-
AADC
-
-
-
-
Aromatic amino acid decarboxylase
-
-
-
-
Aromatic L-amino acid decarboxylase
-
-
-
-
Aromatic L-amino acid decarboxylase
-
-
DOPA decarboxylase
-
-
-
-
Tryptophan decarboxylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-dopa = dopamine + CO2
decarboxylation reaction mechanism, overview. Reaction via a Michaelis complex and a N4'-protonated external aldimine, respectively, the substrate L-dopa preferentially binds unprotonated to the N4'-protonated internal Schiff base
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transamination
half-transamination of D-aromatic amino acid and aromatic amines under anaerobic conditions catalyzed by DDC
Pictet-Spengler cyclization
a reaction occurring at the active site of DDC
decarboxylation
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
Aromatic-L-amino-acid carboxy-lyase
A pyridoxal-phosphate protein. The enzyme also acts on some other aromatic L-amino acids, including L-tryptophan, L-tyrosine and L-phenylalanine.
CAS REGISTRY NUMBER
COMMENTARY
9042-64-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,4-Dihydroxyphenylalanine
3-Hydroxytyramine + CO2
-
-
-
-
?
3,4-Dihydroxyphenylalanine
Dopamine + CO2
-
L-DOPA, substrate exerts apoptotic cytotoxicity towards PC12 cells at a concentration of 0.1-0.2 mM for 24-48 h
major amine neurotransmitter
-
?
L-3,4-Dihydroxyphenylalanine
Dopamine + CO2
-
DOPA, plays a role in the neuromodulation of behavior
-
-
?
L-3,4-Dihydroxyphenylalanine
Dopamine + CO2
-
L-dopa, levodopa, substrate alleviates the clinical symptoms of Parkinson disease
-
-
?
L-3,4-Dihydroxyphenylalanine
Dopamine + CO2
-
the renal dopaminergic system is highly dynamic and the basic mechanisms for the regulation of this system mainly depends on the availability of L-dopa, its fast decarboxylation into dopamine, precise cell outward amine transfer mechanisms, dopamine interaction with specific receptor and accurate intracellular signal transduction
-
-
?
L-tryptophan
tryptamine + CO2
-
enzyme responsible for the decarboxylation step in both the catecholamine and indoleamine synthetic pathway, second step enzyme for monoamine synthesis
-
?
additional information
?
-
-
key enzyme in the production of biogenic 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
-
-
?
additional information
?
-
-
DOPA cyclohexyl ester is an antagonist of DOPA
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,4-Dihydroxyphenylalanine
Dopamine + CO2
-
L-DOPA, substrate exerts apoptotic cytotoxicity towards PC12 cells at a concentration of 0.1-0.2 mM for 24-48 h
major amine neurotransmitter
-
?
L-3,4-Dihydroxyphenylalanine
Dopamine + CO2
-
DOPA, plays a role in the neuromodulation of behavior
-
-
?
L-3,4-Dihydroxyphenylalanine
Dopamine + CO2
-
L-dopa, levodopa, substrate alleviates the clinical symptoms of Parkinson disease
-
-
?
L-3,4-Dihydroxyphenylalanine
Dopamine + CO2
-
the renal dopaminergic system is highly dynamic and the basic mechanisms for the regulation of this system mainly depends on the availability of L-dopa, its fast decarboxylation into dopamine, precise cell outward amine transfer mechanisms, dopamine interaction with specific receptor and accurate intracellular signal transduction
-
-
?
L-tryptophan
tryptamine + CO2
-
enzyme responsible for the decarboxylation step in both the catecholamine and indoleamine synthetic pathway, second step enzyme for monoamine synthesis
-
?
additional information
?
-
-
key enzyme in the production of biogenic 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
-
-
?
additional information
?
-
-
DOPA cyclohexyl ester is an antagonist of DOPA
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
serotonin
and/or its aldehyde, behaves as a mechanism-based inhibitor, product inhibition
3'-hydroxybenzylhydrazine
-
NSD-1015, a central aromatic L-amino acid decarboxylase inhibitor
7-hydroxy-N,N-di-n-propyl-2-aminotetralin
-
reduced AAAD activity in the striatum by acute treatment with the D2-like receptor agonist
bromocryptine
-
reduced AAAD activity in the striatum by acute and chronic treatment with the D2-like receptor agonist
carbidopa
-
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
Clorgyline
-
reduced AAAD activity in the striatum by acute treatment with the dopamine receptor indirect agonist
L-Dopa
-
reduced AAAD activity in the striatum by acute and chronic treatment with the dopamine receptor indirect agonist
Pargyline
-
reduced AAAD activity in the striatum by acute treatment with the dopamine receptor indirect agonist
quinpirole
-
reduced AAAD activity in the striatum by chronic treatment with the D2-like receptor agonist
Benserazide
-
intrastriatal inhibition of the enzyme prevents the appearance of L-dopa-induced dyskinetic movements at the lesioned side
Benserazide
-
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
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
-
additional information
-
a decrease in urinary levels of dopamine and in renal AADC activity at 20 twenty-six weeks after renal mass ablation
-
additional information
-
dopamine receptor activation decreases AAAD activity
-
additional information
-
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.
-
additional information
-
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.
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
amantadine
-
drug acting on glutamatergic receptor type enhances AAAD activity
budipine
-
drug acting on glutamatergic receptor type enhances AAAD activity
clonidine
-
drug acting on alpha adrenergic receptor type enhances AAAD activity
clozapine
-
enhanced AAAD activity in the striatum by acute treatment with the D2-like receptor antagonist
dextrometorphan
-
drug acting on glutamatergic receptor type enhances AAAD activity
haloperidol
-
enhanced AAAD activity in the striatum by acute and chronic treatment with the D2-like receptor antagonist
L-745,870
-
enhanced AAAD activity in the striatum by acute treatment with the D2-like receptor antagonist
L-Dopa
-
L-DOPA treatment (20-200 microM) increases the levels of dopamine by 226%-504% after 3-6 h of treatment and enhances the activities of tyrosine hydroxylase and aromatic L-amino acid decarboxylase
memantine
-
drug acting on glutamatergic receptor type enhances AAAD activity
phencyclidine
-
drug acting on glutamatergic receptor type enhances AAAD activity
pimozide
-
enhanced AAAD activity in the striatum by acute treatment with the D2-like receptor antagonist
pyridoxal 5'-phosphate
-
stimulated by addition of excess pyridoxal phosphate
remoxipride
-
enhanced AAAD activity in the striatum by acute treatment with the D2-like receptor antagonist
SCH 23390
-
enhanced AAAD activity in the striatum by acute and chronic treatment with the D1-like receptor antagonist
SKF 38393
-
enhanced AAAD activity in the striatum by chronic treatment with the D1-like receptor agonist
spiperone
-
enhanced AAAD activity in the striatum by acute and chronic treatment with the D2-like receptor antagonist
sulpiride
-
enhanced AAAD activity by in the striatum by acute and chronic treatment with the D2-like receptor antagonist
flupenthixol
-
enhanced AAAD activity in the striatum by acute treatment with the D2-like receptor antagonist
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.086
L-Dopa
decarboxylation reaction, pH and temperature not specified in the publication
2.2
L-3,4-dihydroxyphenylalanine
-
determined in homogenates of renal cortex of 3/4 nephrectomized rats after 26 weeks
2.6
L-3,4-dihydroxyphenylalanine
-
determined in homogenates of renal cortex of sham surgery rats (control) after 10 weeks
2.6
L-3,4-dihydroxyphenylalanine
-
determined in homogenates of renal cortex of sham surgery rats (control) after 26 weeks
2.9
L-3,4-dihydroxyphenylalanine
-
determined in homogenates of renal cortex of 3/4 nephrectomized rats after 10 weeks
additional information
additional information
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.3
L-Dopa
decarboxylation reaction, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00000113
-
determined in homogenates of renal cortex of 3/4 nephrectomized rats after 26 weeks
0.00001427
-
determined in homogenates of renal cortex of sham surgery rats (control) after 10 weeks
0.00001653
-
determined in homogenates of renal cortex of sham surgery rats (control) after 26 weeks
0.00001893
-
determined in homogenates of renal cortex of 3/4 nephrectomized rats after 10 weeks
0.0325
-
activity of AADC, control level without treatment of L-DOPA in PC-12 cells
additional information
additional information
-
110% activity compared to control level, treatment with 0.02 mM L-DOPA in PC-12 cells at 1 h (time point)
additional information
-
237% activity compared to control level, treatment with 0.02 mM L-DOPA in PC-12 cells at 3 h (time point)
additional information
-
242% activity compared to control level, treatment with 0.1 mM L-DOPA in PC-12 cells at 1 h (time point)
additional information
-
269% activity compared to control level, treatment with f 0.1 mM L-DOPA in PC-12 cells at 3 h (time point)
additional information
-
311% activity compared to control level, treatment with 0.2 mM L-DOPA in PC-12 cells at 1 h (time point)
additional information
-
348% activity compared to control level, treatment with 0.2 mM L-DOPA in PC-12 cells at 3 h (time point)
additional information
-
enzyme activity is closely associated with substrate response and is a determining factor for the formation of dopamine
additional information
-
in striatum and retina, kinetic activation of AAAD is rapid, short-lasting and characterized by changes in the apparent Vmax for both the substrate and the cofactor pyridoxal 5'-phosphate
additional information
-
The activity of AADC begins to decrease to about 177% (0.02 mM L-DOPA), 233% (0.1 mM L-DOPA) and 297% (0.2 mM L-DOPA) of the control levels by 3-6 h, and then returns to control level by about 24-48 h
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
AADC neurons, the shapes and sizes of AADC neurons vary according to their location
-
renal dopaminergic system activity in rat (3/4 nephrectomized) kidney up to 26 weeks after surgery
additional information
immunohistochemic localization study using anti-AADC antibodies with AADC immunoreactivity by the avidin-biotin complex (ABC) peroxidase immunohistochemistry, overview. The diverse morphological characteristics of the AADC cells suggests that they can be further divided into several subtypes
in the gray matter, AADC neurons are not only found in the region around the central canal but also in the dorsal horn, intermediate zone, and ventral horn. In the white matter a large number of glial cells are AADC-immunopositive in different spinal segments and the vast majority of these cells express oligodendrocyte and radial glial phenotypes. Additionally, a small number of AADC neurons are found in the white matter along the ventral median fissure
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
aromatic L-amino acid decarboxylase (AADC) is an essential enzyme in the synthesis of serotonin, dopamine, and certain trace amines and is active in a variety of organs including the brain and spinal cord
physiological function
mammalian Dopa decarboxylase catalyzes the conversion of L-Dopa and L-5 hydroxytryptophan to dopamine and serotonin, respectively. Both of them are biologically active neurotransmitters whose levels has to be finely tuned. Enzyme DDC is not considered to be rate-limiting in physiological catecholamines or indoleamines synthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DDC_RAT
480
0
54053
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
instability of the apo form of aromatic L-amino acid decarboxylase in vivo and in vitro, implications for the involvement of the flexible loop that covers the active site
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AADC expression in the L-DOPA naive 6-hydroxydopamine-lesioned rats does decrease significantly as compared with intact striata
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Bender, D.A.; Coulson, W.F.
Aromatic amino acid decarboxylase: pH-dependence of substrates and inhibitors
Biochem. Soc. Trans.
5
1353-1356
1977
Rattus norvegicus
Ando-Yamamoto, M.; Hayashi, H.; Sugiyama, H.; Fukui, H.; Watanabe, T.; Wada, H.
Purification of L-DOPA decarboxylase from rat liver and production of polyclonal and monoclonal antibodies against it
J. Biochem.
101
405-414
1987
Rattus norvegicus
Dominici, P.; Tancini, B.; Barra, D.; Voltattorni, C.B.
Purification and characterization of rat-liver 3,4-dihydroxyphenylalanine decarboxylase
Eur. J. Biochem.
169
209-213
1987
Rattus norvegicus
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
Dluzen, D.; Reddy, A.; McDermott, J.
The aromatic amino acid decarboxylase inhibitor, NSD-1015, increases release of dopamine: response characteristics
Neuropharmacology
31
1223-1229
1992
Rattus norvegicus
Jebai, F.; Hanoun, N.; Hamon, M.; Thibault, J.; Peltre, G.; Gros, F.; Krieger, M.
Expression, purification, and characterization of rat aromatic L-amino acid decarboxylase in Escherichia coli
Protein Expr. Purif.
11
185-194
1997
Rattus norvegicus
Husebye, E.S.; Boe, A.S.; Rorsman, F.; Kaempe, O.; Aakvaag, A.; Rygh, T.; Flatmark, T.; Haavik, J.
Inhibition of aromatic L-amino acid decarboxylase activity by human autoantibodies
Clin. Exp. Immunol.
120
420-423
2000
Rattus norvegicus
Ishida, Y.; Yokoyama, C.; Inatomi, T.; Yagita, K.; Dong, X.; Yan, L.; Yamaguchi, S.; Nagatsu, I.; Komori, T.; Kitahama, K.; Okamura, H.
Circadian rhythm of aromatic L-amino acid decarboxylase in the rat suprachiasmatic nucleus: gene expression and decarboxylating activity in clock oscillating cells
Genes Cells
7
447-459
2002
Rattus norvegicus
Mura, A.; Linder, J.C.; Young, S.J.; Groves, P.M.
Striatal cells containing aromatic L-amino acid decarboxylase: an immunohistochemical comparison with other classes of striatal neurons
Neuroscience
98
501-511
2000
Rattus norvegicus
Matsuda, N.; Hayashi, H.; Miyatake, S.; Kuroiwa, T.; Kagamiyama, H.
Instability of the apo form of aromatic L-amino acid decarboxylase in vivo and in vitro: implications for the involvement of the flexible loop that covers the active site
J. Biochem.
135
33-42
2004
Rattus norvegicus
Tehranian, R.; Montoya, S.E.; Van Laar, A.D.; Hastings, T.G.; Perez, R.G.
Alpha-synuclein inhibits aromatic amino acid decarboxylase activity in dopaminergic cells
J. Neurochem.
99
1188-1196
2006
Rattus norvegicus
Hadjiconstantinou, M.; Neff, N.H.
Enhancing aromatic L-amino acid decarboxylase activity: implications for L-DOPA treatment in Parkinsons disease
CNS Neurosci. Ther.
14
340-351
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Jin, C.M.; Yang, Y.J.; Huang, H.S.; Lim, S.C.; Kai, M.; Lee, M.K.
Induction of dopamine biosynthesis by l-DOPA in PC12 cells: implications of L-DOPA influx and cyclic AMP
Eur. J. Pharmacol.
591
88-95
2008
Rattus norvegicus
Matsushita, N.; Misu, Y.; Goshima, Y.
In vivo antagonism of the behavioral responses to L-3-,4-dihydroxyphenylalanine by L-3-,4-dihydroxyphenylalanine cyclohexyl ester in conscious rats
Eur. J. Pharmacol.
605
109-113
2009
Rattus norvegicus
Moreira-Rodrigues, M.; Sampaio-Maia, B.; Pestana, M.
Renal dopaminergic system activity in rat remnant kidney up to twenty-six weeks after surgery
Life Sci.
84
409-414
2009
Rattus norvegicus
Buck, K.; Ferger, B.
Intrastriatal inhibition of aromatic amino acid decarboxylase prevents L-DOPA-induced dyskinesia: A bilateral reverse in vivo microdialysis study in 6-hydroxydopamine lesioned rats
Neurobiol. Dis.
29
210-220
2008
Rattus norvegicus
Gil, S.; Park, C.; Lee, J.; Koh, H.
The roles of striatal serotonin and L-amino-acid decarboxylase on L-DOPA-induced dyskinesia in a hemiparkinsonian rat model
Cell. Mol. Neurobiol.
30
817-825
2010
Rattus norvegicus
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)
EXTERNAL LINKS (specific for EC-Number 4.1.1.28)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
