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Information on EC 4.1.1.28 - aromatic-L-amino-acid decarboxylase and Organism(s) Sus scrofa and UniProt Accession P80041
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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: Sus scrofa
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
-
-
-
-
DDC
-
-
-
-
DOPA decarboxylase
-
-
-
-
L-DOPA decarboxylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-dopa = dopamine + CO2
investigation of the mechanism by using the absorption spectrum of the bound coenzyme as an indicator of events
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transamination
half-transamination of D-aromatic amino acid and aromatic amines under anaerobic conditions catalyzed by DDC
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
2-fluoro-L-(3,4-dihydroxyphenyl)alanine
4-(2-aminoethyl)-3-fluorobenzene-1,2-diol + CO2
-
-
-
?
5-fluoro-L-(3,4-dihydroxyphenyl)alanine
5-(2-aminoethyl)-3-fluorobenzene-1,2-diol + CO2
-
-
-
?
5-hydroxytryptamine + O2
5-hydroxyindolacetaldehyde + NH3
-
side reaction, decarboxylation-dependent transamination
-
?
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
-
?
L-(3,4-dihydroxyphenyl)alanine
4-(2-aminoethyl)benzene-1,2-diol + CO2
-
-
-
?
L-threo-(3,4-dihydroxyphenyl)serine
4-[(2-hydroxyethyl)amino]benzene-1,2-diol + 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
-
-
?
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
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
?
-
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
one pyridoxal 5'-phosphate cofactor per dimer structure
pyridoxal 5'-phosphate
-
contains 1 mol of pyridoxal 5'-phosphate per mol of enzyme, nearly complete decarboxylation of L-3,4-dihydroxyphenylalanine in absence of added coenzyme, existence of at least 4 coenzyme-apoenzyme complexes, three of them are active
pyridoxal 5'-phosphate
-
1 mol of pyridoxal 5'-phosphate is bound to the epsilon-amino group of a lysyl residue of the apoenzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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.
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
serotonin
and/or its aldehyde, behaves as a mechanism-based inhibitor, product inhibition
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
L-Dopa
decarboxylation reaction, pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.5
L-Dopa
Y332F DDC mutant, reaction in 50 mM Hepes, pH 7.5, at 25°C causes the production of ammonia and 3,4-dihydroxyphenylacetaldehyde along with the consumption of molecular oxygen in a 1:2 molar ratio
5.8
L-Dopa
decarboxylation reaction, pH and temperature not specified in the publication
additional information
additional information
mutant T246A presents a decarboxylase activity, the kcat value is decreased by 29fold with respect to wild-type
-
additional information
additional information
When 50 microM Y332F DDC is mixed with 0.1 mM L-dopa under single turnover conditions up to 4 sec a gradual conversion of the pyridoxal 5'-phosphate of the enzyme takes place concomitantly to pyridoxamine 5'-phosphate and aldehyde formation while L-dopa is consumed. After 3.6 sec, 23% of the original pyridoxal 5'-phosphate is converted into pyridoxamine 5'-phosphate and 25% of the original L-dopa is transformed into 3,4-dihydroxyphenylacetaldehyde. A pyridoxamine 5'-phosphate intermediate forms during the first catalytic cycle.
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.7
5-hydroxy-L-tryptophan
wild-type enzyme, the data of initial velocity for decarboxylation of 5-hydroxy-L-tryptophan versus substrate concentration exhibit a substrate-inhibition pattern that requires a modified version of the Michaelis-Menten equation.
10
L-Dopa
wild-type enzyme, the data of initial velocity for decarboxylation of L-dopa versus substrate concentration curiously exhibit a substrate-inhibition pattern that requires a modified version of the Michaelis-Menten equation.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
The course of the reaction of Y332 mutant with 0.3 mM L-dopa has been followed at different enzyme concentrations. Although the shapes of the profiles for the interconversion of the 2 coenzymatic forms (pyridoxal 5'-phosphate and pyridoxamine 5'-phosphate) are similar at all the enzyme concentrations tested. At each enzyme concentration there are 2 phases: at first, pyridoxamine 5'-phosphate increases at the expense of pyridoxal 5'-phosphate, and then this tendency is reversed until approximately 85% of the pyridoxal 5'-phosphate cofactor is regenerated, the amount of pyridoxamine 5'-phosphate formed relative to the initial pyridoxal 5'-phosphate content of the enzyme, during consumption of L-dopa, increases as the enzyme concentration decreases. At higher enzyme concentrations, where L-dopa consumption is faster, the accumulation of the pyridoxamine 5'-phosphate-intermediate is less appreciable. In every case the pyridoxamine 5'-phosphate species is generated during the course of linear formation of products.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
both the neuronal and the extraneuronal AADC mRNA isoforms are present at early brain developmental stages in the basal ganglia
-
both the neuronal and the extraneuronal AADC mRNA isoforms are present at early brain developmental stages in the brain stem
-
increase of AADC activity with brain development is considered to be associated with special stages of neuronal maturation and tissue differentiation
-
AADC expression in the developing pig brain is highly expressed in the basal ganglia and the brain stem regions, and also significantly expressed in the cortex, the hippocampus and the cerebellum
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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. The aromatic compounds produced by oxidative deamination through the enzyme possess similar biological activities as the aromatic amines and thus are strong biologically active signals
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_PIG
486
0
53936
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
density functional theory and real-time dynamics studies. In the crystal structure, residue Asp 271 interacts with the pyridine nitrogen atom of pyridoxal 5'-phosphate through H-bonding in both native and substrate-bound enzyme. Residue Thr 246 is in close proximity to the oxygen atom of 3-OH of the pyridoxal 5'-phosphate pyridine ring only in substrate-bound enzyme. In the ligand-free enzyme, this distance is not favorable for hydrogen bonding
modeling of complex with inhibitor epigallocatechin-3-gallate. 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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T246A
T246 act as an essential general base for the oxidative deamination reaction
Y332F
Y332F
wild-type enzyme and Y332F variant are able to perform the oxidation toward aromatic amines or aromatic L-amino acids, without the aid of any cofactor related to oxygen chemistry.
Y332F
the mutant variant switches its reaction specificity from amine generation to aldehyde generation performing an oxidative deamination of L-Dopa
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
reaction specificity with D-aromatic amino acids does not change in presence or absence of O2, the reaction with L-aromatic amino acids seems to be affected by O2
-
649696
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.1 M potassium phosphate buffer, 0.1 mM dithiothreitol, stable for at least 2 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and expression of wild-type DDC and Y332F and T246A mutants in SVS370 Escherichia coli cells.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
development of dopamine treatment ainst Parkinson's disease, drug target for treatment of neurodgenerative diseases
pharmacology
-
biosynthesis of pharmaceutically important monoterpenoid indole alkaloids
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
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
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
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
Voltattorni, C.B.; Giartosio, A.; Turano, C.
Aromatic-L-amino acid decarboxylase from pig kidney
Methods Enzymol.
142
179-187
1987
Sus scrofa
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
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
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
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
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
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
-
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
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)
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
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)
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)
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
Lin, Y.L.; Gao, J.
Kinetic isotope effects of L-Dopa decarboxylase
J. Am. Chem. Soc.
133
4398-4403
2011
Sus scrofa
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)
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)
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
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