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EC Tree
IUBMB Comments A pyridoxal-phosphate protein. Also acts on tyrosine and other aromatic amino acids.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
amino acid decarboxylase, phenylalanine decarboxylase, l-phenylalanine decarboxylase,
more
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amino acid decarboxylase
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Aromatic L-amino acid decarboxylase
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Decarboxylase, phenylalanine
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L-Phenylalanine decarboxylase
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L-tyrosine/L-phenylalanine decarboxylase
bifunctional protein from Enterococcus faecium expressing L-phenylalanine and L-tyrosine decarboxylase activities
phenylalanine decarboxylase 1
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phenylalanine decarboxylase 2
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PDC
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additional information
cf. EC 4.1.1.28
additional information
cf. EC 4.1.1.28
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L-phenylalanine = phenylethylamine + CO2
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L-phenylalanine carboxy-lyase (phenylethylamine-forming)
A pyridoxal-phosphate protein. Also acts on tyrosine and other aromatic amino acids.
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3,4-Dihydroxyphenylalanine
Dopamine + CO2
5-Hydroxytryptophan
Serotonin + CO2
Histidine
Histamine + CO2
L-phenylalanine
phenylethylamine + CO2
L-Tyrosine
Tyramine + CO2
Phenylalanine
?
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?
S-(E-1,2-Dichlorovinyl)-L-cysteine
?
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?
Tryptophan
Tryptamine + CO2
additional information
?
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3,4-Dihydroxyphenylalanine
Dopamine + CO2
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?
3,4-Dihydroxyphenylalanine
Dopamine + CO2
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?
3,4-Dihydroxyphenylalanine
Dopamine + CO2
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?
3,4-Dihydroxyphenylalanine
Dopamine + CO2
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?
3,4-Dihydroxyphenylalanine
Dopamine + CO2
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?
3,4-Dihydroxyphenylalanine
Dopamine + CO2
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?
3,4-Dihydroxyphenylalanine
Dopamine + CO2
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?
5-Hydroxytryptophan
Serotonin + CO2
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?
5-Hydroxytryptophan
Serotonin + CO2
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?
5-Hydroxytryptophan
Serotonin + CO2
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?
5-Hydroxytryptophan
Serotonin + CO2
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?
5-Hydroxytryptophan
Serotonin + CO2
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?
5-Hydroxytryptophan
Serotonin + CO2
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?
5-Hydroxytryptophan
Serotonin + CO2
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?
Histidine
Histamine + CO2
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?
Histidine
Histamine + CO2
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?
L-phenylalanine
phenylethylamine + CO2
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?
L-phenylalanine
phenylethylamine + CO2
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?
L-phenylalanine
phenylethylamine + CO2
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?
L-phenylalanine
phenylethylamine + CO2
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?
L-phenylalanine
phenylethylamine + CO2
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?
L-phenylalanine
phenylethylamine + CO2
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?
L-phenylalanine
phenylethylamine + CO2
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?
L-phenylalanine
phenylethylamine + CO2
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L-phenylalanine
phenylethylamine + CO2
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?
L-phenylalanine
phenylethylamine + CO2
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L-Tyrosine
Tyramine + CO2
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?
L-Tyrosine
Tyramine + CO2
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?
L-Tyrosine
Tyramine + CO2
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?
L-Tyrosine
Tyramine + CO2
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?
L-Tyrosine
Tyramine + CO2
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?
L-Tyrosine
Tyramine + CO2
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L-Tyrosine
Tyramine + CO2
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?
Tryptophan
Tryptamine + CO2
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Tryptophan
Tryptamine + CO2
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Tryptophan
Tryptamine + CO2
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Tryptophan
Tryptamine + CO2
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Tryptophan
Tryptamine + CO2
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Tryptophan
Tryptamine + CO2
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?
additional information
?
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involved in amine formation from natural amino acids prior to excretion
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?
additional information
?
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Micrococcus percitreus
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involved in biosynthesis of aromatic amines
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?
additional information
?
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enzyme PDC from Pseudomonas putida is active on L-amino acids and shows higher substrate specificity for phenylalanine than for tyrosine
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additional information
?
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enzyme PDC from Pseudomonas putida is active on L-amino acids and shows higher substrate specificity for phenylalanine than for tyrosine
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?
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L-phenylalanine
phenylethylamine + CO2
Phenylalanine
?
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?
additional information
?
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L-phenylalanine
phenylethylamine + CO2
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?
L-phenylalanine
phenylethylamine + CO2
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L-phenylalanine
phenylethylamine + CO2
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?
additional information
?
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involved in amine formation from natural amino acids prior to excretion
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?
additional information
?
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Micrococcus percitreus
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involved in biosynthesis of aromatic amines
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?
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
Micrococcus percitreus
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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increase of activity towards S-(E-1,2-dichlorovinyl)-L-cysteine
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5-Aminooxymethyl-2-bromophenol
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brocresine, 75 mg/kg body mass cause 98% inhibition of liver enzyme in vivo
5-hydroxytryptophan
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complete inhibition at 0.001 mM
alpha-Methyl-3,4-dihydroxyphenylalanine
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competitive
alpha-Methyl-5-hydroxyphenylalanine
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alpha-Methyl-m-tyrosine
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alpha-Methyltryptophan
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N1-(DL-Seryl)-N2-(2,3,4)-trihydroxybenzyl hydrazine
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50 mg/kg cause 99% inhibition of liver enzyme in vivo
p-chloromercuribenzoate
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complete inhibition at 0.01 mM
tryptamine
Micrococcus percitreus
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42% inhibition at 0.1% v/v
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Benzene
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stimulates decarboxylation of natural amino acids
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Ataxia
Gene Therapy in Movement Disorders: A Systematic Review of Ongoing and Completed Clinical Trials.
Carcinogenesis
Glycine decarboxylase is an unusual amino acid decarboxylase involved in tumorigenesis.
Carcinoid Tumor
[Amino acid decarboxylase in pheochromocytoma and carcinoid tissue.]
Cerebral Palsy
Therapy of intention myoclonus with L-5-hydroxytryptophan and a peripheral decarboxylase inhibitor, MK 486.
Dyskinesias
[Serum dopamine-beta-hydroxylase, glutamic acid decarboxylase and 1-aromatic amino acid decarboxylase in involuntary movement disorders (author's transl)]
Dystonia
Gene Therapy in Movement Disorders: A Systematic Review of Ongoing and Completed Clinical Trials.
Dystonia
Syndromic intellectual disability: A new phenotype caused by an aromatic amino acid decarboxylase gene (DDC) variant.
Huntington Disease
Gene Therapy in Movement Disorders: A Systematic Review of Ongoing and Completed Clinical Trials.
Hypotension, Orthostatic
L-dihydroxyphenylserine (Droxidopa): a new therapy for neurogenic orthostatic hypotension: the US experience.
Hypothyroidism
TSH and prolactin stimulation by the decarboxylase inhibitor benserazide in primary hypothyroidism.
Lung Neoplasms
Expression in human lung cancer cell lines of genes of prohormone processing and the neuroendocrine phenotype.
Migraine Disorders
A genetic analysis of serotonergic biosynthetic and metabolic enzymes in migraine using a DNA pooling approach.
Movement Disorders
Gene Therapy in Movement Disorders: A Systematic Review of Ongoing and Completed Clinical Trials.
Movement Disorders
[Serum dopamine-beta-hydroxylase, glutamic acid decarboxylase and 1-aromatic amino acid decarboxylase in involuntary movement disorders (author's transl)]
Multiple System Atrophy
Gene Therapy in Movement Disorders: A Systematic Review of Ongoing and Completed Clinical Trials.
Muscle Hypotonia
Syndromic intellectual disability: A new phenotype caused by an aromatic amino acid decarboxylase gene (DDC) variant.
Myoclonus
Therapy of intention myoclonus with L-5-hydroxytryptophan and a peripheral decarboxylase inhibitor, MK 486.
Neoplasms
Characterization of neuroblastic tumors using 18F-FDOPA PET.
Neoplasms
Expression in human lung cancer cell lines of genes of prohormone processing and the neuroendocrine phenotype.
Neoplasms
Fluorescence and electron microscopic histochemistry of endocrine-like cells in gastric mucosa and argyrophil tumor of Praomys (Mastomys) natalensis. Analysis of 5-hydroxytryptamine, histamine, Histidine decarboxylase, and aromatic amino acid decarboxylase.
Neoplasms
Use of radiolabeled monofluoromethyl-Dopa to define the subunit structure of human L-Dopa decarboxylase.
Neuroendocrine Tumors
Characterization of neuroblastic tumors using 18F-FDOPA PET.
Neuroendocrine Tumors
The effects of molar activity on [18F]FDOPA uptake in patients with neuroendocrine tumors.
Neurologic Manifestations
Syndromic intellectual disability: A new phenotype caused by an aromatic amino acid decarboxylase gene (DDC) variant.
Paralysis
Gene Therapy in Movement Disorders: A Systematic Review of Ongoing and Completed Clinical Trials.
Parkinson Disease
Cheminformatics and virtual screening studies of COMT inhibitors as potential Parkinson's disease therapeutics.
Parkinson Disease
Effect of tolcapone on plasma levodopa concentrations after coadministration with levodopa/carbidopa to healthy volunteers.
Parkinson Disease
Gene Therapy in Movement Disorders: A Systematic Review of Ongoing and Completed Clinical Trials.
Parkinson Disease
Increased neostriatal dopamine activity after intraperitoneal or intranasal administration of L-DOPA: on the role of benserazide pretreatment.
Parkinson Disease
Mucuna pruriens in Parkinson Disease: A Kinetic-Dynamic Comparison With Levodopa Standard Formulations.
phenylalanine decarboxylase deficiency
Corrigendum to "Aromatic amino acid decarboxylase deficiency: Molecular and metabolic basis and therapeutic outlook" [Mol Genet Metab. 2019 May;127(1):12-22].
Pheochromocytoma
Use of radiolabeled monofluoromethyl-Dopa to define the subunit structure of human L-Dopa decarboxylase.
Pheochromocytoma
[Amino acid decarboxylase in pheochromocytoma and carcinoid tissue.]
Small Cell Lung Carcinoma
Expression in human lung cancer cell lines of genes of prohormone processing and the neuroendocrine phenotype.
Supranuclear Palsy, Progressive
Gene Therapy in Movement Disorders: A Systematic Review of Ongoing and Completed Clinical Trials.
Tremor
Gene Therapy in Movement Disorders: A Systematic Review of Ongoing and Completed Clinical Trials.
Tremor
Therapy of intention myoclonus with L-5-hydroxytryptophan and a peripheral decarboxylase inhibitor, MK 486.
tryptophan 5-monooxygenase deficiency
Role of brain cytochrome P450 (CYP2D) in the metabolism of monoaminergic neurotransmitters.
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0.04
3,4-dihydroxyphenylalanine
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0.066
5-hydroxytryptamine
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cloned enzyme
0.002
5-hydroxytryptophan
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0.14
L-dihydroxyphenylalanine
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cloned enzyme
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0.0008
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D,L-phenylalanine
0.0054
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S-(E-1,2-dichlorovinyl)-L-cysteine
0.93
Micrococcus percitreus
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cell-cycle-dependend
1813
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5-hydroxytryptamine, cloned enzyme
8444
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L-dihydroxyphenylalanine, cloned enzyme
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9
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9
Micrococcus percitreus
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30
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30
Micrococcus percitreus
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37
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enzyme assay at
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dog
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guinea pig
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strain RM58, previously named strain BIFI-85
UniProt
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human
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Micrococcus percitreus
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no activity in Papaver somniferum
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UniProt
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UniProt
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rat
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saccharata group, cv. Zlota Karlowa
UniProt
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commercial preparation
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physiological function
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enzyme expression in Escherichia coli blocks motility and results in a 50fold decrease in the expression of class 2 and class 3 flagellar genes fliA and fliC, respectively. The expression of flhDC encoding the class 1 activator of the flagellarcascade is unchanged by the expression at both the transcriptional and translational levels. Phenethylamine, a decarboxylation product derived from phenylalanine, is able to mimic the overexpression and decrease both motility and class 2/3 flagellar gene expression. Both enzyme overexpression and phenethylamine strongly inhibit biofilm formation in Escherichia coli. Enzyme overexpression and exogenous phenethylamine can also reduce motility in other enteric bacteria, but have no effect on motility in non-enteric Gram-negative bacteria
metabolism
the enzyme is involved in biosynthesis and trunover of 2-phenylethylamine in maize
metabolism
the enzyme is involved in biosynthesis and turnover of 2-phenylethylamine in maize
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A0A0B2NPZ9_GLYSO
124
0
14222
TrEMBL
other Location (Reliability: 3 )
Q1JTV5_ENTFC
625
0
70330
TrEMBL
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A0A0B2S3E8_GLYSO
485
0
54699
TrEMBL
other Location (Reliability: 3 )
A0A1D6FGI6_MAIZE
258
0
29111
TrEMBL
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A0A1D6H1J3_MAIZE
260
0
29187
TrEMBL
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Q88JU5_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
470
0
51444
TrEMBL
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additional information
genes PDC, TDC, TAL, SHT, and THT are introduced into engineered Escherichia coli strain HP-2 to synthesize N-(p-coumaroyl) phenethylamine and N-(p-coumaroyl) tyramine, method evaluation and optimization, overview. p-Coumaric acid is synthesized from tyrosine by TAL and phenethylamine is synthesized from phenylalanine by PDC. Therefore, the intracellular concentrations of both tyrosine and phenylalanine are critical for the final yield of N-(p-coumaroyl) phenethylamine
additional information
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genes PDC, TDC, TAL, SHT, and THT are introduced into engineered Escherichia coli strain HP-2 to synthesize N-(p-coumaroyl) phenethylamine and N-(p-coumaroyl) tyramine, method evaluation and optimization, overview. p-Coumaric acid is synthesized from tyrosine by TAL and phenethylamine is synthesized from phenylalanine by PDC. Therefore, the intracellular concentrations of both tyrosine and phenylalanine are critical for the final yield of N-(p-coumaroyl) phenethylamine
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3¦C, 0.03 M phosphate buffer, pH 7, 40% loss of activity after 10 days, purified enzyme
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brain stem enzyme, partial
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expressed in Escherichia coli
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expressed in Escherichia coli strain DH5alphaF'
gene PDC, recombinant expression in Escherichia coli strain HP-2, coexpression with genes TDC, TAL, SHT, and THT
gene PDC1, enzyme expression analysis
gene PDC2, enzyme expression analysis
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methyl jasmonate elicitation causes various changes in the contents of PEA, PAA and PE in the maize seedlings. Methyl jasmonate treatments leads to high upregulation of most genes in the 2-phenethylamine metabolism, including genes PDC1 and PDC2, with the exception of three genes (i.e. ADH1, ADH2 and AO2) whose expression is downregulated. One-day methyl jasmonate treatment (10-6 and 10-4 M) increases the PDC1 expression 1.3-10.2fold, whereas a 4-day exposure leads to 1.1fold and 3.1fold increased expression levels, respectively, compared to controls
methyl jasmonate elicitation causes various changes in the contents of PEA, PAA and PE in the maize seedlings. Methyl jasmonate treatments leads to high upregulation of most genes in the 2-phenethylamine metabolism, including genes PDC1 and PDC2, with the exception of three genes (i.e. ADH1, ADH2 and AO2) whose expression is downregulated. One-day methyl jasmonate treatment (10-6 and 10-4 M) increases the PDC2 expression 1.2-3.3fold, whereas a 4-day exposure leads to 1.1fold and 2.5fold increased expression levels, respectively, compared to controls
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analysis
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use of enzyme for decarboxylation of phenylalanine to increase its volatility for continuous-flow isotopic analysis without introducing extraneous C or significant isotopic fractionation
pharmacology
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side-effects of pharmacologically active decarboxylation products considered
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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
brenda
Lovenberg, W.; Weissbach, H.; Udenfriend, S.
Aromatic L-amino acid decarboxylase
J. Biol. Chem.
237
89-93
1962
Canis lupus, Cavia aperea
brenda
David, J.C.; Dairman, W.; Udenfriend, S.
On the importance of decarboxylation in the metabolism of phenylalanine, tyrosine, and tryptophan
Arch. Biochem. Biophys.
160
561-568
1974
Homo sapiens, Rattus norvegicus
brenda
Chen, K.C.S.; Holmes, K.K.
A rapid procedure for detection of bacterial amino acid decarboxylases
Anal. Biochem.
111
60-66
1981
Morganella morganii
brenda
Buckberry, L.D.; Patel, R.; Hollingworth, L.; Teesdale-Spittle, P.H.
Cysteine conjugate beta-lyase activity of amino acid decarboxylase
Biochem. Soc. Trans.
26
269
1998
Enterococcus faecalis
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brenda
Nakazawa, H.; Sano, K.; Kumagai, H.; Yamada, H.
Distribution and formation of aromatic L-amino acid decarboxylase in bacteria
Agric. Biol. Chem.
41
2241-2247
1977
Achromobacter sp., Micrococcus percitreus, Micrococcus sp., Sarcina sp., Staphylococcus sp.
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Taylor, D.C.; Whightman, F.
Metabolism of D,L-chlorophenylalanines by phenylalanine aminotransferase isozymes purified from bushbean shoots
Biochemistry
26
1279-1288
1987
no activity in Papaver somniferum, Phaseolus vulgaris
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brenda
Ziadeh, B.I.; Michaud, A.L.; Saad, N.M.R.; Lewis, B.A.; Rafii, M.; Pencharz, P.B.; Brenna, J.T.
Enzymatic decarboxylation of tyrosine and phenylalanine to enhance volatility for high-precision isotopic analysis
Anal. Chem.
74
479-483
2002
Enterococcus faecalis
brenda
Marcobal, A.; de las Rivas, B.; Munoz, R.
First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
FEMS Microbiol. Lett.
258
144-149
2006
Enterococcus faecium (Q1JTV5), Enterococcus faecium
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Stevenson, L.G.; Szostek, B.A.; Clemmer, K.M.; Rather, P.N.
Expression of the DisA amino acid decarboxylase from Proteus mirabilis inhibits motility and class 2 flagellar gene expression in Escherichia coli
Res. Microbiol.
164
31-37
2013
Proteus mirabilis
brenda
Sytykiewicz, H.; Horbowicz, M.; Wiczkowski, W.; Koczkodaj, D.; Mitrus, J.; Sawicki, T.; Slawianowska, J.; Szwed, M.
Methyl jasmonate elicitation affects expression of genes involved in biosynthesis and turnover of 2-phenylethylamine in maize seedlings
Acta Biol. Crac. Ser. Bot.
58
67-80
2016
Zea mays subsp. mays (A0A1D6FGI6), Zea mays subsp. mays (A0A1D6H1J3)
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brenda
Sim, G.; Yang, S.; Kim, B.; Ahn, J.
Bacterial synthesis of N-hydroxycinnamoyl phenethylamines and tyramines
Microb. Cell Fact.
14
162
2015
Pseudomonas putida (Q88JU5), Pseudomonas putida ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440 (Q88JU5)
brenda
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