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Information on EC 4.3.1.24 - phenylalanine ammonia-lyase and Organism(s) Petroselinum crispum and UniProt Accession P24481
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4.3.1.24 phenylalanine ammonia-lyaseIUBMB Comments
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) and EC 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family . This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine . The enzyme from some species is highly specific for phenylalanine [7,8].
Specify your search results
Word Map
- 4.3.1.24
- phenol
-
phenylpropanoids
- polyphenols
- flavonoid
- seedling
- chalcone
- elicitors
- lignin
-
cinnamic
- cultivar
-
4.3.1.5
- anthocyanins
- jasmonate
- chitinase
-
postharvest
-
4-hydroxylase
-
trans-cinnamic
-
defense-related
-
p-coumaric
-
phytoalexins
-
pathogenesis-related
-
lignification
-
chlorogenic
- phytophthora
- petroselinum
- parsley
- 4-coumarate
- phenylketonuria
- crispum
-
fresh-cut
-
elicitor-induced
-
wall-bound
- dihydroflavonol
-
elicitor-treated
-
4-coumarate:coa
- polyphenoloxidase
- glutinis
-
4-reductase
- rhodotorula
- rhodosporidium
- synthesis
- 3-o-glucosyltransferase
- d-phenylalanine
- pharmacology
- dehydroalanine
- medicine
-
hydroxycinnamoyl
- monolignols
- analysis
- food industry
- drug development
- agriculture
-
syringyl
- biotechnology
- lindemuthianum
- glycinea
-
matricaria
- cinnamoyl-coa
- nutrition
The taxonomic range for the selected organisms is: Petroselinum crispum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phenylalanine ammonia-lyase, phenylalanine ammonia lyase, l-phenylalanine ammonia-lyase, dcpal1, phe ammonia-lyase, rgpal, avpal, palrs1, atpal2, sspal1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine ammonia-lyase (trans-cinnamate-forming)
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) and EC 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). 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 [9]. The enzyme from some species is highly specific for phenylalanine [7,8].
CAS REGISTRY NUMBER
COMMENTARY
9024-28-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-chloro-trans-cinnamate + NH3
2-chloro-L-phenylalanine
50.5% conversion
-
-
?
2-fluoro-trans-cinnamate + NH3
2-fluoro-L-phenylalanine
95.8% conversion
-
-
?
2-hydroxy-trans-cinnamate + NH3
2-hydroxy-L-phenylalanine
15.5% conversion
-
-
?
2-methoxy-trans-cinnamate + NH3
2-methoxy-L-phenylalanine
54.6% conversion
-
-
?
3-chloro-trans-cinnamate + NH3
3-chloro-L-phenylalanine
91.7% conversion
-
-
?
3-fluoro-trans-cinnamate + NH3
3-fluoro-L-phenylalanine
52.1% conversion
-
-
?
3-hydroxy-trans-cinnamate + NH3
3-hydroxy-L-phenylalanine
85.7% conversion
-
-
?
3-methoxy-trans-cinnamate + NH3
3-methoxy-L-phenylalanine
85.7% conversion
-
-
?
4-chloro-trans-cinnamate + NH3
4-chloro-L-phenylalanine
89.1% conversion
-
-
?
4-fluoro-trans-cinnamate + NH3
4-fluoro-L-phenylalanine
65.9% conversion
-
-
?
4-hydroxy-trans-cinnamate + NH3
4-hydroxy-L-phenylalanine
0.8% conversion
-
-
?
4-methoxy-trans-cinnamate + NH3
4-methoxy-L-phenylalanine
6.4% conversion
-
-
?
L-phenylalanine
trans-cinnamate + NH3
the enzyme is specific for L-phenylalanine
-
-
r
(1,1'-biphenyl)acrylic acid + NH3
([1,1'-biphenyl]-4-yl)alanine
-
no product is detected with wild-type enzyme or either single mutants, 8% conversion with mutant enzyme F137A/I460V after 20 h
-
-
?
(2'-chloro-5-phenylthiophen-2-yl)acrylic acid + NH3
(2'-chloro-5-phenylthiophen-2-yl)alanine
-
no product is detected with wild-type enzyme or either single mutants, 2% conversion with mutant enzyme F137A/I460V after 20 h
-
-
?
(2'-chloro-5-phenylthiophen-2-yl)alanine
(2'-chloro-5-phenylthiophen-2-yl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion
-
-
?
(2-phenylthiazol-4-yl)alanine
(2-phenylthiazol-4-yl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutant F137A provides low high conversion
-
-
?
(2E)-3-(1-benzofuran-2-yl)acrylic acid + NH3
2-amino-3-(1-benzofuran-2-yl)propanoic acid
-
-
-
-
r
(2E)-3-(1-benzothien-2-yl)acrylic acid + NH3
2-amino-3-(1-benzothien-2-yl)propanoic acid
-
-
-
-
r
(2E)-3-(2-furyl)acrylic acid + NH3
(S)-2-amino-3-(2-furyl)propanoic acid
-
-
-
-
r
(2E)-3-(2-thienyl)acrylic acid + NH3
2-amino-3-(2-thienyl)propanoic acid
-
-
-
-
r
(2E)-4-amino-cinnamic acid + NH3
4-amino-L-phenylalanine
-
poor substrate
-
-
r
(2E)-4-trifluoromethyl-cinnamic acid + NH3
4-trifluoromethyl-L-phenylalanine
-
poor substrate
-
-
r
(3-methoxy)alanine
(3-methoxy)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion
-
-
?
(4'-chloro-5-phenylthiophen-2-yl)alanine
(4'-chloro-5-phenylthiophen-2-yl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion
-
-
?
(4'-fluoro-[1,1'-biphenyl]-4-yl)acrylic acid + NH3
(4'-fluoro-[1,1'-biphenyl]-4-yl)alanine
-
no product is detected with wild-type enzyme or either single mutants, 6% conversion with mutant enzyme F137A/I460V after 20 h
-
-
?
(4'-fluoro-[1,1'-biphenyl]-4-yl)alanine
(4'-fluoro-[1,1'-biphenyl]-4-yl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion. 39% conversion with with mutant enzyme F137A/I460V, 18% conversion with mutant enzyme F137A/L138V, 15% conversion with mutant enzyme F137A
-
-
?
(5-phenylthiophen-2-yl)acrylic acid + NH3
(5-phenylthiophen-2-yl)alanine
-
no product is detected with wild-type enzyme or either single mutants, 6% conversion with mutant enzyme F137A/I460V after 20 h
-
-
?
(5-phenylthiophen-2-yl)alanine
(5-phenylthiophen-2-yl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion. 48% conversion with mutant enzyme F137A/L138V, 44% conversion with mutant enzyme F137
-
-
?
(naphthalen-2-yl)alanine
(naphthalen-2-yl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion
-
-
?
(styryl)acrylic acid + NH3
(styryl)alanine
-
no product is detected with wild-type enzyme or either single mutants, but 22% and 27%, respectively, conversion can be achieved with the F137V/I460V and F137V/I460A double mutants
-
-
?
(styryl)alanine
(styryl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion
-
-
?
([1,1'-biphenyl]-4-yl)alanine
(1,1'-biphenyl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion
-
-
?
2,3,4,5,6-pentafluoro-L-phenylalanine
2,3,4,5,6-pentafluoro-trans-cinnamate + NH3
-
-
-
r
2,6-difluoro-L-phenylalanine
2,6-difluoro-trans-cinnamate + NH3
-
-
-
r
2-amino-3-(1-benzofuran-2-yl)propanoic acid
(2E)-3-(1-benzofuran-2-yl)acrylic acid + NH3
-
49% of the rate with L-phenylalanine
-
-
r
2-amino-3-(1-benzothien-2-yl)propanoic acid
(2E)-3-(1-benzothien-2-yl)acrylic acid + NH3
-
14% of the rate with L-phenylalanine
-
-
r
2-amino-3-(2-furyl)propanoic acid
(2E)-3-(2-furyl)acrylic acid + NH3
-
34% of the rate with L-phenylalanine
-
-
r
2-amino-3-(2-thienyl)propanoic acid
(2E)-3-(2-thienyl)acrylic acid + NH3
-
101% of the rate with L-phenylalanine
-
-
r
2-amino-3-(3-thienyl)propanoic acid
(2E)-3-(3-thienyl)acrylic acid + NH3
-
16% of the rate with L-phenylalanine
-
-
r
3,5-difluoro-L-phenylalanine
3,5-difluoro-trans-cinnamate + NH3
-
-
-
r
4-trifluoromethyl-L-phenylalanine
4-trifluoromethyl-(E)-cinnamate + NH3
-
-
-
-
r
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
(2E,4E)-5-(4-chlorophenyl)penta-2,4-dienoic acid + NH3
-
-
-
-
?
rac-(E)-2-amino-5-phenylpent-4-enoic acid
(2E,4E)-5-phenylpenta-2,4-dienoic acid + NH3
-
-
-
-
?
additional information
?
-
-
no substrate: 2-amino-3-(3-furyl)propanoic acid. Enzyme acts selectively on L-amino acids and their derivatives
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
reaction can be reversed by applying high concentrations of ammonia
-
?
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
reversibility of the reaction is demonstrated for the natural substrate L-Phe at an ammonium carbonate concentration as low as 0.1 M
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,5-dihydro-5-methylidene-4H-imidazol-4-one
-
electrophilic prosthetic group
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0783
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
-
pH 8.8, 30°C, mutant enzyme F137V
0.154
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
-
pH 8.8, 30°C, wild-type enzyme
0.201
rac-(E)-2-amino-5-phenylpent-4-enoic acid
-
pH 8.8, 30°C, mutant enzyme F137V
0.395
rac-(E)-2-amino-5-phenylpent-4-enoic acid
-
pH 8.8, 30°C, wild-type enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00024
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
-
pH 8.8, 30°C, wild-type enzyme
0.0786
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
-
pH 8.8, 30°C, mutant enzyme F137V
0.0062
rac-(E)-2-amino-5-phenylpent-4-enoic acid
-
pH 8.8, 30°C, wild-type enzyme
0.276
rac-(E)-2-amino-5-phenylpent-4-enoic acid
-
pH 8.8, 30°C, mutant enzyme F137V
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
-
pH 8.8, 30°C, wild-type enzyme
1.004
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
-
pH 8.8, 30°C, mutant enzyme F137V
0.0156
rac-(E)-2-amino-5-phenylpent-4-enoic acid
-
pH 8.8, 30°C, wild-type enzyme
1.373
rac-(E)-2-amino-5-phenylpent-4-enoic acid
-
pH 8.8, 30°C, mutant enzyme F137V
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PAL1_PETCR
716
0
77829
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure. The active state of enzyme is a Tyr110-loop-in conformation and opening-closing the entrance to the active site may happen by a breathing motion of this loop. Comparison with strucutural models of Photorhabdus luminescens and Streptomyces maritimus enzymes
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F137A
-
mutation increased the activity significantly towards almost all non-natural analogues of phenylalanine compared to the wild-type enzyme. Moderate enhancement (15%) of the conversion in ammonia elimination from (4'-fluoro-[1,1'-biphenyl]-4-yl)alanine and for (5-phenylthiophen-2-yl)alanine (44%)
F137A/L138V
-
moderate enhancement (18%) of the conversion in ammonia elimination from (4'-fluoro-[1,1'-biphenyl]-4-yl)alanine and for (5-phenylthiophen-2-yl)alanine (48%)
F137V
F137V/I460V
-
moderate enhancement (39%) of the conversion in ammonia elimination from (4'-fluoro-[1,1'-biphenyl]-4-yl)alanine
I460A
-
mutation increased the activity significantly towards almost all non-natural analogues of phenylalanine compared to the wild-type enzyme, mutation decreases the Tm value significantly from 75°C to 51°C
I460V
-
mutation increased the activity significantly towards almost all non-natural analogues of phenylalanine compared to the wild-type enzyme
L137H
-
mutation almost doubles the kinetic D-isotope effect compared to wild-type enzyme
L137H/Q487E
-
mutation almost doubles the kinetic D-isotope effect compared to wild-type enzyme
Q487A
-
kinetic D isotope effect is of the same magnitude as wild-type enzyme
Y350F
-
kinetic D isotope effect is of the same magnitude as wild-type enzyme
additional information
F137V
-
mutation increased the activity significantly towards almost all non-natural analogues of phenylalanine compared to the wild-type enzyme
F137V
-
the mutant enzyme can transform L-styrylalanine with comparable activity to that of the wild-type enzyme with L-phenylalanine. Ammonia elimination from L-styrylalanine by the non-mutated wild-type enzyme takes place with a 777fold lower kcat/KM value than the deamination of the natural substrate, L-phenylalanine. The mutant enzyme shows enhanced catalytic efficiency in the ammonia elimination reaction of several racemic styrylalanine derivatives
additional information
a Tyr10-loop-in conformation of the enzyme structure is constructed by partial homology modeling, and the static and dynamic behavior of the loop-in/loop-out structures are compared
additional information
-
a Tyr10-loop-in conformation of the enzyme structure is constructed by partial homology modeling, and the static and dynamic behavior of the loop-in/loop-out structures are compared
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
fusion proteins with gluthatione S-transferase expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
enzyme substitution therapy for the treatment of phenylketonuria
pharmacology
-
enzyme substitution therapy for the treatment of phenylketonuria
synthesis
-
use of enzyme for production of enantiopure D- and L-heteroaryl-2-alanines, i.e. R- and S-2-amino-3-(heteroaryl)propanoic acids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hanson, K.R.; Havir, E.A.
Phenylalanine ammonia-lyase
Biochem. Plants
7
577-625
1981
Avena sativa, Ricinus communis, Cucumis sativus, Dunaliella marina, Fagopyrum esculentum, Glycine max, Helianthus annuus, Hordeum vulgare, Ipomoea batatas, Nasturtium officinale, Petroselinum crispum, Petunia x hybrida, Quercus pedunculata, Rhizoctonia solani, Sinapis alba, Solanum tuberosum, Sorghum bicolor, Spinacia oleracea, Streptomyces verticillatus, Triticum aestivum, Tropaeolum majus, Zea mays
-
Appert, C.; Logermann, E.; Hahlbrock, K.; Schmid, J.; Amrhein, N.
Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley (Petroselinum crispum Nym.)
Eur. J. Biochem.
225
491
1994
Petroselinum crispum
Gloge, A.; Zon, J.; Kovari, A.; Poppe, L.; Retey, J.
Phenylalanine ammonia-lyase: the use of its broad substrate specificity for mechanistic investigations and biocatalysis--synthesis of L-arylalanines
Chem. Eur. J.
6
3386-3390
2000
Petroselinum crispum
Viergutz, S.; Poppe, L.; Tomin, A.; Retey, J.
Mechanistic investigation of phenylalanine ammonia lyase by using N-methylated phenylalanines
Helv. Chim. Acta
86
3601-3612
2003
Petroselinum crispum
-
Appert, C.; Zon, J.; Amrhein, N.
Kinetic analysis of the inhibition of phenylalanine ammonia-lyase by 2-aminoindan-2-phosphonic acid and other phenylalanine analogues
Phytochemistry
62
415-422
2003
Petroselinum crispum
Viergutz, S.; Retey, J.
Kinetic analysis of the reactions catalyzed by histidine and phenylalanine ammonia lyases
Chem. Biodivers.
1
296-302
2004
Petroselinum crispum
Pilbak, S.; Tomin, A.; Retey, J.; Poppe, L.
The essential tyrosine-containing loop conformation and the role of the C-terminal multi-helix region in eukaryotic phenylalanine ammonia-lyases
FEBS J.
273
1004-1019
2006
Photorhabdus luminescens, Streptomyces maritimus, Petroselinum crispum (P24481), Petroselinum crispum
Paizs, C.; Katona, A.; Retey, J.
The interaction of heteroaryl-acrylates with phenylalanine ammonia-lyase from parsley
Chem. Eur. J.
12
2739-2744
2006
Petroselinum crispum
Bartsch, S.; Bornscheuer, U.
Mutational analysis of phenylalanine ammonia lyase to improve reactions rates for various substrates
Protein Eng. Des. Sel.
23
929-933
2010
Petroselinum crispum
Weiser, D.; Bencze, L.C.; Banoczi, G.; Ender, F.; Kiss, R.; Kokai, E.; Szilagyi, A.; Vertessy, B.G.; Farkas, O.e.; Paizs, C.; Poppe, L.
Phenylalanine ammonia-lyase-catalyzed deamination of an acyclic amino acid enzyme mechanistic studies aided by a novel microreactor filled with magnetic nanoparticles
ChemBioChem
16
2283-2288
2015
Petroselinum crispum
Filip, A.; Nagy, E.Z.A.; Tork, S.D.; Banoczi, G.; To?a, M.I.; Irimie, F.D.; Poppe, L.; Paizs, C.; Bencze, L.C.
Tailored mutants of phenylalanine ammonia-lyase from Petroselinum crispum for the synthesis of bulky L- and D-arylalanines
ChemCatChem
10
2627-2633
2018
Petroselinum crispum
Dressen, A.; Hilberath, T.; Mackfeld, U.; Billmeier, A.; Rudat, J.; Pohl, M.
Phenylalanine ammonia lyase from Arabidopsis thaliana (AtPAL2) A potent MIO-enzyme for the synthesis of non-canonical aromatic alpha-amino acids Part I Comparative characterization to the enzymes from Petroselinum crispum (PcPAL1) and Rhodosporidium to the enzymes from Petroselinum crispum (PcPAL1) and Rhodosporidium toruloides (RtPAL)
J. Biotechnol.
258
148-157
2017
Petroselinum crispum (P24481), Petroselinum crispum, Arabidopsis thaliana (P45724), Arabidopsis thaliana
Bencze, L.C.; Filip, A.; Banoczi, G.; Tosa, M.I.; Irimie, F.D.; Gellert, A.; Poppe, L.; Paizs, C.
Expanding the substrate scope of phenylalanine ammonia-lyase from Petroselinum crispum towards styrylalanines
Org. Biomol. Chem.
15
3717-3727
2017
Petroselinum crispum
Kong, J.
Phenylalanine ammonia-lyase, a key component used for phenylpropanoids production by metabolic engineering
RSC Adv.
5
62587-62603
2015
Synechocystis sp., Arabidopsis thaliana, Oscillatoria sp., Petroselinum crispum, Photorhabdus luminescens, Streptomyces verticillatus, Trifolium pratense, Streptomyces maritimus, Rubrobacter xylanophilus, Albuca bracteata, Leptolyngbya sp., Salvia miltiorrhiza (A9XIW5), Salvia miltiorrhiza (C7E4J2), Salvia miltiorrhiza (U3N6Q1), Nostoc punctiforme (B2J528), Melissa officinalis (E1UYU6), Rhodotorula mucilaginosa (P10248), Trichormus variabilis (Q3M5Z3), Rhodotorula glutinis (V5TFQ0)
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EXTERNAL LINKS (specific for EC-Number 4.3.1.24)
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Release 2023.1 (January 2023)
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