Information on EC 4.3.1.25 - phenylalanine/tyrosine ammonia-lyase

for references in articles please use BRENDA:EC4.3.1.25
Word Map on EC 4.3.1.25
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


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

top print hide
EC NUMBER
COMMENTARY hide
4.3.1.25
-
top print hide
RECOMMENDED NAME
GeneOntology No.
phenylalanine/tyrosine ammonia-lyase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-phenylalanine = trans-cinnamate + NH3
show the reaction diagram
L-tyrosine = trans-p-hydroxycinnamate + NH3
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination of NH3
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
benzoate biosynthesis II (CoA-independent, non-beta-oxidative)
-
-
coumarins biosynthesis (engineered)
-
-
ephedrine biosynthesis
-
-
naringenin biosynthesis (engineered)
-
-
phenylpropanoid biosynthesis, initial reactions
-
-
suberin monomers biosynthesis
-
-
trans-cinnamoyl-CoA biosynthesis
-
-
Phenylalanine metabolism
-
-
Phenylpropanoid biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine(or L-tyrosine):trans-cinnamate(or trans-p-hydroxycinnamate) ammonia-lyase
This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase), EC 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.24 (phenylalanine ammonia-lyase). The enzyme from some monocots, including maize, and from the yeast Rhodosporidium toruloides, deaminate L-phenylalanine and L-tyrosine with similar catalytic efficiency [3]. The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family [3]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [4].
top
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform PAL4
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
IFO 0559
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Phe
(E)-cinnamate + NH3
show the reaction diagram
L-phenylalanine
(E)-cinnamate + NH3
show the reaction diagram
L-Tyr
p-coumarate + NH3
show the reaction diagram
-
-
-
?
L-tyrosine
p-coumarate + NH3
show the reaction diagram
L-tyrosine
p-hydroxycinnamic acid + NH3
show the reaction diagram
L-tyrosine
trans-p-hydroxycinnamate + NH3
show the reaction diagram
-
-
-
-
?
trans-cinnamate + NH3
L-Phe
show the reaction diagram
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
show the reaction diagram
additional information
?
-
-
no substrate: L-histidine
-
-
-
top print hide
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
L-phenylalanine
(E)-cinnamate + NH3
show the reaction diagram
top print hide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
slight stimulation
Mg2+
-
slight stimulation
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxycinnamic acid
-
-
4-coumarate
5,5'-dithiobis(2-nitrobenzoate)
-
-
Acetic anhydride
Aminooxyacetate
-
-
benzyl alcohol
-
-
Br-
-
competitive
Cinnamic acid
Cl-
-
competitive
Co2+
-
strong
Cu2+
-
strong
D-Phe
dihydrocaffeic acid
-
-
DL-2-hydroxyphenylalanine
-
-
Fe3+
-
strong
fluorophenylalanine
-
-
glycine
-
3.54 mM, 50% inhibition
I-
-
competitive
L-beta-phenyllactic acid
-
-
L-phenylserine
-
-
m-cresol
-
9.9 mM, 50% inhibition
m-cresol/glycine
-
0.387 mM, 50% inhibition, strong synergistic inhibition
-
Ni2+
-
strong
o-Cresol
-
2.93 mM, 50% inhibition
o-cresol/glycine
-
0.078 mM, 50% inhibition, strong synergistic inhibition
-
p-chloromercuribenzoate
-
-
p-cresol/glycine
-
1.03 mM, 50% inhibition
-
p-hydroxymercuribenzoate
-
-
phenol
-
3.89 mM, 50% inhibition
phenol/glycine
-
0.056 mM 50% inhibition, strong synergistic inhibition
-
phenylpyruvate
trinitrobenzene sulfonic acid
Zn2+
-
weak
additional information
-
not inhibited by p-cresol
-
top print hide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chitohexaose hydrochloride
-
chitosan hexamer, activation of PAL in leaves
chitopentaose hydrochloride
-
chitosanpentamer, activation of PAL in leaves
chitotetraose hydrochloride
-
chitosan tetramer, activation of PAL in leaves
hexa-N-acetyl-chitohexaose
-
chitin hexamer, activation of PAL in leaves
Mn2+
-
stabilization of enzyme
penta-N-acetyl-chitopentaose
-
chitin tetramer, activation of PAL in leaves
tetra-N-acetyl-chitotetraose
-
chitin pentamer, activation of PAL in leaves
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25 - 2.07
L-Phe
0.126 - 2.33
L-phenylalanine
0.085 - 0.18
L-Tyr
0.044 - 0.615
L-tyrosine
4.2
trans-cinnamate
-
-
top print hide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.32
L-Phe
pH 8.5, 37°C
1.53 - 9.8
L-phenylalanine
0.54
L-Tyr
pH 8.5, 37°C
0.53 - 1.44
L-tyrosine
top print hide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.88
L-Phe
pH 8.5, 37°C
5.56
L-Tyr
pH 8.5, 37°C
top print hide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2
glycine
-
25°C, pH 8.8
2.85
m-cresol
-
25°C, pH 8.8
0.3
m-cresol/glycine
-
25°C, pH 8.8
-
0.8
o-Cresol
-
25°C, pH 8.8
0.038
o-cresol/glycine
-
25°C, pH 8.8
-
2.1
phenol
-
25°C, pH 8.8
0.014
phenol/glycine
-
25°C, pH 8.8
-
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9.5
-
above 88% of maximum activity
10
-
80% of maximum activity
12
-
12% of maximum activity
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
-
isoelectric focusing
top print hide
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
in shoot and branch shoot, mainly loclaized to sclerenchymal cells
Manually annotated by BRENDA team
top print hide
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
-
2 * 58000 + 2 * 68000, SDS-PAGE
68000
-
2 * 58000 + 2 * 68000, SDS-PAGE
70000
-
x * 70000, SDS-PAGE
73500
-
4 * 73500, SDS-PAGE
75711
4 * 75711, calculated
80000
-
2 * 80000, SDS-PAGE
83000
-
x * 83000, SDS-PAGE
86000
-
4 * 86000, SDS-PAGE
165000
-
gel filtration, equilibrium sedimentation
248000
-
non-denaturing PAGE
250000
-
gel filtration
275000 - 300000
-
-
275000
-
sucrose density gradient centrifugation
290000
gel filtration
300000
-
gel filtration
330000
-
gel filtration
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 80000, SDS-PAGE
tetramer
top print hide
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
top print hide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
10 min, stable
70
-
10 min, complete inactivation
additional information
-
L-Phe increases thermostability
top print hide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-60°C, enzyme concentration 20-40 mg/ml, stable for 6 months
-
-80°C, 50 mM Tris, pH 8.5, 25% glycerol, stable
-
0-2°C, 50 mM Tris/HCl, 0.01% Mn2+, pH 8.8, whole cells retain 85% of initial enzyme activity for at least 12 weeks
-
4°C, 50 mM Tris, pH 8.5, stable for at least a month
-
4°C, stable for at least 1 month
-
top print hide
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
controlled expression in Escherichia coli to mitigate product toxicity
expression in Escherichia coli
expression in Pseudomonas putida strain S12
-
top print hide
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
rapid quantization of Phe and Tyr in plasma and serum from subjects with phenylketonuria
synthesis
top
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 4.3.1.25)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)