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
Rhodosporidium toruloides
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
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
Rhodosporidium toruloides
-
-
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, 37C
1.53 - 9.8
L-phenylalanine
0.54
L-Tyr
Bambusa oldhamii
D5KS97
pH 8.5, 37C
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, 37C
203
5.56
L-Tyr
Bambusa oldhamii
D5KS97
pH 8.5, 37C
415
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2
glycine
-
25C, pH 8.8
2.85
m-cresol
-
25C, pH 8.8
0.3
m-cresol/glycine
-
25C, pH 8.8
-
0.8
o-Cresol
-
25C, pH 8.8
0.038
o-cresol/glycine
-
25C, pH 8.8
-
2.1
Phenol
-
25C, pH 8.8
0.014
phenol/glycine
-
25C, 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
PDB
SCOP
CATH
ORGANISM
UNIPROT
Rhodosporidium toruloides
Rhodosporidium toruloides
Rhodosporidium toruloides
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
165000
Rhodosporidium toruloides
-
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
Rhodosporidium toruloides
-
2 * 80000, SDS-PAGE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Rhodosporidium toruloides
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
Rhodosporidium toruloides
-
10 min, stable
70
Rhodosporidium toruloides
-
10 min, complete inactivation
additional information
Rhodosporidium toruloides
-
L-Phe increases thermostability
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-60C, enzyme concentration 20-40 mg/ml, stable for 6 months
-
-80C, 50 mM Tris, pH 8.5, 25% glycerol, stable
-
0-2C, 50 mM Tris/HCl, 0.01% Mn2+, pH 8.8, whole cells retain 85% of initial enzyme activity for at least 12 weeks
-
4C, 50 mM Tris, pH 8.5, stable for at least a month
-
4C, stable for at least 1 month
Rhodosporidium toruloides
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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