Information on EC 4.3.1.25 - phenylalanine/tyrosine ammonia-lyase

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

EC NUMBER
COMMENTARY hide
4.3.1.25
-
RECOMMENDED NAME
GeneOntology No.
phenylalanine/tyrosine ammonia-lyase
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination of NH3
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
benzoate biosynthesis II (CoA-independent, non-beta-oxidative)
-
-
Biosynthesis of secondary metabolites
-
-
coumarins biosynthesis (engineered)
-
-
ephedrine biosynthesis
-
-
Metabolic pathways
-
-
naringenin biosynthesis (engineered)
-
-
Phenylalanine metabolism
-
-
Phenylpropanoid biosynthesis
-
-
phenylpropanoid biosynthesis, initial reactions
-
-
suberin monomers biosynthesis
-
-
trans-cinnamoyl-CoA biosynthesis
-
-
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].
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
strain S12
-
-
Manually annotated by BRENDA team
strain S12
-
-
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
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
trans-cinnamate + NH3
show the reaction diagram
L-phenylalanine
trans-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
-
-
-
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
trans-cinnamate + NH3
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
slight stimulation
Mg2+
-
slight stimulation
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
-
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
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
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.32
L-Phe
Bambusa oldhamii
D5KS97
pH 8.5, 37°C
1.53 - 9.8
L-phenylalanine
0.54
L-Tyr
Bambusa oldhamii
D5KS97
pH 8.5, 37°C
0.53 - 1.44
L-tyrosine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.88
L-Phe
Bambusa oldhamii
D5KS97
pH 8.5, 37°C
203
5.56
L-Tyr
Bambusa oldhamii
D5KS97
pH 8.5, 37°C
415
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
-
isoelectric focusing
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
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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 80000, SDS-PAGE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
10 min, stable
70
-
10 min, complete inactivation
additional information
-
L-Phe increases thermostability
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
controlled expression in Escherichia coli to mitigate product toxicity
expression in Escherichia coli
expression in Pseudomonas putida strain S12
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
rapid quantization of Phe and Tyr in plasma and serum from subjects with phenylketonuria
synthesis