Information on EC 4.1.1.53 - phenylalanine decarboxylase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.1.1.53
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RECOMMENDED NAME
GeneOntology No.
phenylalanine decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-phenylalanine = phenylethylamine + CO2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-phenylalanine degradation IV (mammalian, via side chain)
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Phenylalanine metabolism
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phenylethanol biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine carboxy-lyase (phenylethylamine-forming)
A pyridoxal-phosphate protein. Also acts on tyrosine and other aromatic amino acids.
CAS REGISTRY NUMBER
COMMENTARY hide
9075-72-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
dog
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Manually annotated by BRENDA team
guinea pig
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Manually annotated by BRENDA team
strain RM58, previously named strain BIFI-85
UniProt
Manually annotated by BRENDA team
human
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Manually annotated by BRENDA team
Micrococcus percitreus
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Papaver somniferum
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
rat
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Manually annotated by BRENDA team
Sarcina sp.
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,4-Dihydroxyphenylalanine
Dopamine + CO2
show the reaction diagram
5-Hydroxytryptophan
Serotonin + CO2
show the reaction diagram
Histidine
Histamine + CO2
show the reaction diagram
L-phenylalanine
phenylethylamine + CO2
show the reaction diagram
L-Tyrosine
Tyramine + CO2
show the reaction diagram
Phenylalanine
?
show the reaction diagram
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S-(E-1,2-Dichlorovinyl)-L-cysteine
?
show the reaction diagram
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Tryptophan
?
show the reaction diagram
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Tryptophan
Tryptamine + CO2
show the reaction diagram
Tyrosine
?
show the reaction diagram
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additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Phenylalanine
?
show the reaction diagram
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Tryptophan
?
show the reaction diagram
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Tyrosine
?
show the reaction diagram
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additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Benzene
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stimulates decarboxylation of natural amino acids
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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2.2
histidine
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0.14
L-dihydroxyphenylalanine
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cloned enzyme
1.3
p-tyrosine
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2
phenylalanine
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0.3
tryptophan
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0008
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D,L-phenylalanine
0.0015
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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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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enzyme assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
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enzyme assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
3¦C, 0.03 M phosphate buffer, pH 7, 40% loss of activity after 10 days, purified enzyme
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
brain stem enzyme, partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli strain DH5alphaF'
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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