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
4.3.1.25
-
RECOMMENDED NAME
GeneOntology No.
phenylalanine/tyrosine ammonia-lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-phenylalanine = trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
L-phenylalanine = trans-cinnamate + NH3
show the reaction diagram
ordered uni-bi reaction sequence
-
L-tyrosine = trans-p-hydroxycinnamate + NH3
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PAL/TAL
-
-
-
PAL4
D5KS97
-
phenylalanine-trosine ammonia lyase
-
-
phenylalanine-trosine ammonia lyase
-
-
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform PAL4
UniProt
Manually annotated by BRENDA team
Merr.cv. OAC Bayfield
-
-
Manually annotated by BRENDA team
strain S12
-
-
Manually annotated by BRENDA team
enzyme expression is induced up to 3fold by presence of L-isoleucine, L-phenylalanine or L-tyrosine in growth medium. The presence of trans-cinnamic acid suppresses enzyme expression
-
-
Manually annotated by BRENDA team
Sporobolomyces pararoseus
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
-
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
r
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
Sporobolomyces pararoseus
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
Sporobolomyces pararoseus
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
D5KS97
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
?, r
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Rhodotorula glutinis RE4607095D
-
-
-
-
r
L-Tyr
p-coumarate + NH3
show the reaction diagram
D5KS97
-
-
-
?
L-tyrosine
p-coumarate + NH3
show the reaction diagram
-
-
-
-
?
L-tyrosine
p-coumarate + NH3
show the reaction diagram
-
-
-
?
L-tyrosine
p-coumarate + NH3
show the reaction diagram
-
L-Tyr
-
?
L-tyrosine
p-coumarate + NH3
show the reaction diagram
-
L-Tyr, 50% of the activity with L-Phe
-
-
-
L-tyrosine
p-coumarate + NH3
show the reaction diagram
-
substrate binding is cooperative, nH 2.6
-
-
?
L-tyrosine
p-hydroxycinnamic acid + NH3
show the reaction diagram
-
-
-
-
?
trans-cinnamate + NH3
L-Phe
show the reaction diagram
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
show the reaction diagram
Rhodotorula glutinis, Rhodotorula glutinis RE4607095D
-
-
-
-
r
L-tyrosine
trans-p-hydroxycinnamate + NH3
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no substrate: L-histidine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
slight stimulation
Mg2+
-
slight stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-hydroxycinnamic acid
Sporobolomyces pararoseus
-
-
4-coumarate
Sporobolomyces pararoseus
-
-
4-coumarate
-
-
4-coumarate
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
Acetic anhydride
-
-
Acetic anhydride
-
-
Aminooxyacetate
-
-
benzyl alcohol
Sporobolomyces pararoseus
-
-
Br-
-
competitive
Cinnamic acid
-
trans-cinnamic acid
Cinnamic acid
Sporobolomyces pararoseus
-
-
Cinnamic acid
-
-
Cl-
-
competitive
CN-
Sporobolomyces pararoseus
-
-
CN-
Sporobolomyces pararoseus
-
the substrate analog DL-2-hydroxyphenylalanine or cinnamate protects
Co2+
-
strong
Cu2+
-
strong
dihydrocaffeic acid
-
-
DL-2-hydroxyphenylalanine
-
-
Fe3+
-
strong
fluorophenylalanine
-
-
Gly
Sporobolomyces pararoseus
-
-
glycine
-
3.54 mM, 50% inhibition
Hg2+
-
strong
I-
-
competitive
L-beta-phenyllactic acid
Sporobolomyces pararoseus
-
-
L-phenylserine
-
-
m-cresol
-
9.9 mM, 50% 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
-
-
phenylpyruvate
-
-
trinitrobenzene sulfonic acid
Sporobolomyces pararoseus
-
-
trinitrobenzene sulfonic acid
-
2,4,6-trinitrobenzenesulfonic acid
Tyr
-
D-Tyr; m-Try
Tyr
-
L-Tyr
Zn2+
-
weak
m-cresol/glycine
-
0.387 mM, 50% inhibition, strong synergistic inhibition
-
additional information
-
not inhibited by p-cresol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
0.27
L-Phe
-
-
0.3
L-Phe
Sporobolomyces pararoseus
-
-
2.07
L-Phe
D5KS97
pH 8.5, 37C
0.126
L-phenylalanine
-
pH 9.5
0.161
L-phenylalanine
-
pH 9.5, 35C
0.183
L-phenylalanine
-
pH 8.5
2.33
L-phenylalanine
-
pH 8.5
0.085
L-Tyr
Sporobolomyces pararoseus
-
-
0.097
L-Tyr
D5KS97
pH 8.5, 37C
0.15
L-Tyr
-
-
0.044
L-tyrosine
-
pH 9.5, 35C
0.0677
L-tyrosine
-
pH 9.5
0.432
L-tyrosine
-
pH 8.5
0.615
L-tyrosine
-
pH 8.5
4.2
trans-Cinnamate
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16.32
L-Phe
D5KS97
pH 8.5, 37C
1.53
L-phenylalanine
-
pH 9.5
1.6
L-phenylalanine
-
pH 8.5
3.3
L-phenylalanine
-
pH 9.5, 35C
9.8
L-phenylalanine
-
pH 8.5
0.54
L-Tyr
D5KS97
pH 8.5, 37C
0.53
L-tyrosine
-
pH 8.5
0.93
L-tyrosine
-
pH 9.5
1.3
L-tyrosine
-
pH 9.5, 35C
1.44
L-tyrosine
-
pH 8.5
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.88
L-Phe
D5KS97
pH 8.5, 37C
203
5.56
L-Tyr
D5KS97
pH 8.5, 37C
415
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 9.5
-
above 88% of maximum activity
10
-
80% of maximum activity
12
-
12% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
D5KS97
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
D5KS97
in shoot and branch shoot, mainly loclaized to sclerenchymal cells
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
165000
-
gel filtration, equilibrium sedimentation
34355
248000
-
non-denaturing PAGE
34339
250000
-
gel filtration
34339
275000 - 300000
-
-
34334
275000
Sporobolomyces pararoseus
-
sucrose density gradient centrifugation
34348
290000
D5KS97
gel filtration
716457
294000
-
PAGE
679579
300000
Sporobolomyces pararoseus
-
gel filtration
34348
330000
-
gel filtration
34365
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 70000, SDS-PAGE
?
-
x * 83000, SDS-PAGE
dimer
-
2 * 80000, SDS-PAGE
tetramer
-
4 * 86000, SDS-PAGE
tetramer
-
2 * 58000 + 2 * 68000, SDS-PAGE
tetramer
-
4 * 73500, SDS-PAGE
tetramer
D5KS97
4 * 75711, calculated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
10 min, stable
34355
60
-
3 h, no loss of activity, 4 h, 72% residual activity
679588
60
-
4 h, 10% residual activity
679588
70
-
10 min, complete inactivation
34355
additional information
-
L-Phe increases thermostability
34355
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, 50 mM Tris, pH 8.5, 25% glycerol, stable
-
4C, 50 mM Tris, pH 8.5, stable for at least a month
-
4C, stable for at least 1 month
-
-60C, enzyme concentration 20-40 mg/ml, stable for 6 months
-
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Sporobolomyces pararoseus
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
D5KS97
controlled expression in Escherichia coli to mitigate product toxicity
-
expression in Pseudomonas putida strain S12
-
controlled expression in Escherichia coli to mitigate product toxicity
-
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
rapid quantization of Phe and Tyr in plasma and serum from subjects with phenylketonuria
synthesis
-
immobilization of Escherichia coli cells stably expressing the enzyme on calcium alginate beads for use in batch coversion of L-tyrosine to p-hydroxycinnamic acid. Immobilization and controlling of pH value to 9.8 results in stabilization. In 1 l batch reactions, 50 g/l tyrosine can be converted to 39 g/l p-hydroxycinnamic acid
synthesis
-
use of enzyme for synthesis of optically pure L-phenylalanine from trans-cinnamate
synthesis
Rhodotorula glutinis RE4607095D
-
use of enzyme for synthesis of optically pure L-phenylalanine from trans-cinnamate
-