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Information on EC 4.3.1.25 - phenylalanine/tyrosine ammonia-lyase for references in articles please use BRENDA:EC4.3.1.25Word Map on EC 4.3.1.25
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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phenylalanine/tyrosine ammonia-lyase
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L-phenylalanine = trans-cinnamate + NH3
L-tyrosine = trans-p-hydroxycinnamate + NH3
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-
-
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L-phenylalanine = trans-cinnamate + NH3
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-
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L-phenylalanine = trans-cinnamate + NH3
ordered uni-bi reaction sequence
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benzoate biosynthesis II (CoA-independent, non-beta-oxidative)
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coumarins biosynthesis (engineered)
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ephedrine biosynthesis
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naringenin biosynthesis (engineered)
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phenylpropanoid biosynthesis, initial reactions
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rosmarinic acid biosynthesis I
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suberin monomers biosynthesis
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trans-cinnamoyl-CoA biosynthesis
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Phenylalanine metabolism
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Phenylpropanoid biosynthesis
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Biosynthesis of secondary metabolites
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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].
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phenylalanine-trosine ammonia lyase
PAL
-
-
PAL/TAL
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-
phenylalanine-trosine ammonia lyase
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-
phenylalanine-trosine ammonia lyase
-
-
-
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isoform PAL4
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
IFO 0559
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-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Merr.cv. OAC Bayfield
-
-
brenda
-
-
-
brenda
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
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-
brenda
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L-Phe
(E)-cinnamate + NH3
L-phenylalanine
(E)-cinnamate + NH3
L-Tyr
p-coumarate + NH3
-
-
-
?
L-tyrosine
p-coumarate + NH3
L-tyrosine
p-hydroxycinnamic acid + NH3
L-tyrosine
trans-p-hydroxycinnamate + NH3
-
-
-
-
?
trans-cinnamate + NH3
L-Phe
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
additional information
?
-
-
no substrate: L-histidine
-
-
-
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
-
L-Phe
(E)-cinnamate + NH3
-
-
-
-
r
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?, r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
r
L-tyrosine
p-coumarate + NH3
-
substrate binding is cooperative, nH 2.6
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-
?
L-tyrosine
p-coumarate + NH3
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-
-
?
L-tyrosine
p-coumarate + NH3
-
L-Tyr
-
?
L-tyrosine
p-coumarate + NH3
-
L-Tyr
-
-
-
L-tyrosine
p-coumarate + NH3
-
50% of the activity with L-Phe
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-
L-tyrosine
p-coumarate + NH3
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-
-
-
?
L-tyrosine
p-hydroxycinnamic acid + NH3
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-
-
-
?
L-tyrosine
p-hydroxycinnamic acid + NH3
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-
-
-
?
trans-cinnamate + NH3
L-phenylalanine
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-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
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-
-
-
r
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L-phenylalanine
(E)-cinnamate + NH3
L-phenylalanine
(E)-cinnamate + NH3
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-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
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Ba2+
-
slight stimulation
Mg2+
-
slight stimulation
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2-hydroxycinnamic acid
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-
5,5'-dithiobis(2-nitrobenzoate)
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-
DL-2-hydroxyphenylalanine
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-
glycine
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3.54 mM, 50% inhibition
L-beta-phenyllactic acid
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-
m-cresol
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9.9 mM, 50% inhibition
m-cresol/glycine
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0.387 mM, 50% inhibition, strong synergistic inhibition
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o-Cresol
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2.93 mM, 50% inhibition
o-cresol/glycine
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0.078 mM, 50% inhibition, strong synergistic inhibition
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p-chloromercuribenzoate
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p-cresol/glycine
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1.03 mM, 50% inhibition
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p-hydroxymercuribenzoate
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phenol
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3.89 mM, 50% inhibition
phenol/glycine
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0.056 mM 50% inhibition, strong synergistic inhibition
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trinitrobenzene sulfonic acid
additional information
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not inhibited by p-cresol
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4-coumarate
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Acetic anhydride
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Cinnamic acid
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Cinnamic acid
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trans-cinnamic acid
CN-
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NaCN
CN-
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the substrate analog DL-2-hydroxyphenylalanine or cinnamate protects
D-Phe
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Hg2+
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strong
phenylpyruvate
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trinitrobenzene sulfonic acid
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2,4,6-trinitrobenzenesulfonic acid
trinitrobenzene sulfonic acid
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-
Tyr
-
L-Tyr
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chitohexaose hydrochloride
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chitosan hexamer, activation of PAL in leaves
chitopentaose hydrochloride
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chitosanpentamer, activation of PAL in leaves
chitotetraose hydrochloride
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chitosan tetramer, activation of PAL in leaves
hexa-N-acetyl-chitohexaose
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chitin hexamer, activation of PAL in leaves
Mn2+
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stabilization of enzyme
penta-N-acetyl-chitopentaose
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chitin tetramer, activation of PAL in leaves
tetra-N-acetyl-chitotetraose
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chitin pentamer, activation of PAL in leaves
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0.126 - 2.33
L-phenylalanine
0.25
L-Phe
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-
0.126
L-phenylalanine
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pH 9.5
0.161
L-phenylalanine
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pH 9.5, 35°C
0.183
L-phenylalanine
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pH 8.5
2.33
L-phenylalanine
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pH 8.5
0.085
L-Tyr
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-
0.044
L-tyrosine
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pH 9.5, 35°C
0.0677
L-tyrosine
-
pH 9.5
0.432
L-tyrosine
-
pH 8.5
0.615
L-tyrosine
-
pH 8.5
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1.53 - 9.8
L-phenylalanine
1.53
L-phenylalanine
-
pH 9.5
1.6
L-phenylalanine
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pH 8.5
3.3
L-phenylalanine
-
pH 9.5, 35°C
9.8
L-phenylalanine
-
pH 8.5
0.53
L-tyrosine
-
pH 8.5
1.3
L-tyrosine
-
pH 9.5, 35°C
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1.2
glycine
-
25°C, pH 8.8
2.85
m-cresol
-
25°C, pH 8.8
0.3
m-cresol/glycine
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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
-
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additional information
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-
additional information
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-
additional information
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-
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8.5
-
35°C
8.8
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-
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8 - 9.5
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above 88% of maximum activity
10
-
80% of maximum activity
12
-
12% of maximum activity
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5.8
-
isoelectric focusing
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brenda
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brenda
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brenda
-
brenda
in shoot and branch shoot, mainly loclaized to sclerenchymal cells
brenda
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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
275000
-
sucrose density gradient centrifugation
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dimer
-
2 * 80000, SDS-PAGE
?
-
x * 70000, SDS-PAGE
tetramer
4 * 75711, calculated
tetramer
-
4 * 73500, SDS-PAGE
tetramer
-
2 * 58000 + 2 * 68000, SDS-PAGE
tetramer
-
4 * 86000, SDS-PAGE
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70
-
10 min, complete inactivation
additional information
-
L-Phe increases thermostability
60
-
3 h, no loss of activity, 4 h, 72% residual activity
60
-
4 h, 10% residual activity
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-60°C, enzyme concentration 20-40 mg/ml, stable for 6 months
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-80°C, 50 mM Tris, pH 8.5, 25% glycerol, stable
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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
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4°C, 50 mM Tris, pH 8.5, stable for at least a month
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4°C, stable for at least 1 month
-
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-
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controlled expression in Escherichia coli to mitigate product toxicity
expression in Escherichia coli
expression in Pseudomonas putida strain S12
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controlled expression in Escherichia coli to mitigate product toxicity
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controlled expression in Escherichia coli to mitigate product toxicity
-
expression in Escherichia coli
-
expression in Escherichia coli
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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
-
use of enzyme for synthesis of optically pure L-phenylalanine from trans-cinnamate
-
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PALY_MAIZE
703
74927
Swiss-Prot
PALY_RHOTO
716
76880
Swiss-Prot
Q8E9B0_SHEON
Shewanella oneidensis (strain MR-1)
521
56985
TrEMBL
D5KS97_BAMOL
701
75711
TrEMBL
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Camm, E.L.; Towers, G.H.N.
Phenylalanine ammonia lyase
Phytochemistry
12
961-973
1973
Sporidiobolus pararoseus, Triticum aestivum
-
brenda
Hanson, K.R.; Havir, E.A.
Phenylalanine ammonia-lyase
Biochem. Plants
7
577-625
1981
Rhodotorula glutinis
-
brenda
Jorrin, J.; Lopez-Valbuena, R.; Tena, M.
Purification and properties of phenylalanine ammonia-lyase from sunflower (Helianthus annuus L.) hypocotyls
Biochim. Biophys. Acta
964
73-82
1988
Helianthus annuus
-
brenda
Abell, C.W.; Shen, R.S.
Phenylalanine ammonia-lyase from the yeast Rhodotorula glutinis
Methods Enzymol.
142
242-249
1987
Rhodotorula glutinis
brenda
Fritz, R.R.; Hodgins, D.S.; Abell, C.W.
Phenylalanine ammonia-lyase. Induction and purification from yeast and clearance in mammals
J. Biol. Chem.
251
4646-4650
1976
Rhodotorula glutinis
brenda
Jangaard, N.O.
The characterization of phenylalanine ammonia-lyase from several plant species
Phytochemistry
13
1765-1768
1974
Cyperus rotundus, Echinochloa crus-galli, Glycine max, Sorghum halepense, Zea mays
-
brenda
Parkhurst, J.R.; Hodgins, D.S.
Yeast phenylalanine ammonia-lyase. Properties of the enzyme from Sporobolomyces pararoseus and its catalytic site
Arch. Biochem. Biophys.
152
597-605
1972
Sporidiobolus pararoseus
brenda
Hodgins, D.S.
Properties of yeast L-phenylalanine ammonia-lyase
Arch. Biochem. Biophys.
149
91-96
1972
Rhodotorula glutinis
brenda
Vance, C.P.; Bandoni, R.J.; Towers, G.H.N.
Further observations on phenylalanine ammonia-lyase in fungi
Phytochemistry
14
1513-1514
1975
Nectria cinnabarina
-
brenda
Adachi, O.; Matsushita, K.; Shinagawa, E.; Ameyama, M.
Crystallization and properties of L-phenylalanine ammonia-lyase from Rhodosporidium toruloides
Agric. Biol. Chem.
54
2839-2843
1990
Rhodotorula toruloides
-
brenda
Dahiya, J.S.
Isolation and characterization of phenylalanine ammonia-lyase enzyme from the fungus Leptosphaeria maculans
Indian J. Exp. Biol.
31
874-877
1993
Leptosphaeria maculans
-
brenda
Alunni, S.; Cipiciani, A.; Fioroni, G.; Ottavi, L.
Mechanisms of inhibition of phenylalanine ammonia-lyase by phenol inhibitors and phenol/glycine synergistic inhibitors
Arch. Biochem. Biophys.
412
170-175
2003
Rhodotorula glutinis
brenda
Khan, W.; Prithiviraj, B.; Smith, D.L.
Chitosan and chitin oligomers increase phenylalanine ammonia-lyase and tyrosine ammonia-lyase activities in soybean leaves
J. Plant Physiol.
160
859-863
2003
Glycine max
brenda
Trotman, R.J.; Camp, C.E.; Ben-Bassat, A.; DiCosimo, R.; Huang, L.; Crum, G.A.; Sariaslani, F.S.; Haynie, S.L.
Calcium alginate bead immobilization of cells containing tyrosine ammonia lyase activity for use in the production of p-hydroxycinnamic acid
Biotechnol. Prog.
23
638-644
2007
Rhodotorula glutinis
brenda
Vannelli, T.; Xue, Z.; Breinig, S.; Qi, W.W.; Sariaslani, F.S.
Functional expression in Escherichia coli of the tyrosine-inducible tyrosine ammonia-lyase enzyme from yeast Trichosporon cutaneum for production of p-hydroxycinnamic acid
Enzyme Microb. Technol.
41
413-422
2007
Cutaneotrichosporon cutaneum
-
brenda
Xue, Z.; McCluskey, M.; Cantera, K.; Ben-Bassat, A.; Sariaslani, F.S.; Huang, L.
Improved production of p-hydroxycinnamic acid from tyrosine using a novel thermostable phenylalanine/tyrosine ammonia lyase enzyme
Enzyme Microb. Technol.
42
58-64
2007
Phanerochaete chrysosporium, Rhodotorula glutinis
-
brenda
Wall, M.J.; Quinn, A.J.; DCunha, G.B.
Manganese (Mn2+)-dependent storage stabilization of Rhodotorula glutinis phenylalanine ammonia-lyase activity
J. Agric. Food Chem.
56
894-902
2008
Rhodotorula glutinis
brenda
Verhoef, S.; Ballerstedt, H.; Volkers, R.J.; de Winde, J.H.; Ruijssenaars, H.J.
Comparative transcriptomics and proteomics of p-hydroxybenzoate producing Pseudomonas putida S12: novel responses and implications for strain improvement
Appl. Microbiol. Biotechnol.
87
679-690
2010
Pseudomonas putida, Pseudomonas putida S12
brenda
Hsieh, L.S.; Ma, G.J.; Yang, C.C.; Lee, P.D.
Cloning, expression, site-directed mutagenesis and immunolocalization of phenylalanine ammonia-lyase in Bambusa oldhamii
Phytochemistry
71
1999-2009
2010
Bambusa oldhamii (D5KS97)
brenda
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