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Information on EC 4.3.1.24 - phenylalanine ammonia-lyase and Organism(s) Arabidopsis thaliana and UniProt Accession P35510
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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].
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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: Arabidopsis thaliana
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
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
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-fluoro-trans-cinnamate + NH3
2-fluoro-L-phenylalanine
96.1% conversion
-
-
?
2-hydroxy-trans-cinnamate + NH3
2-hydroxy-L-phenylalanine
22.0% conversion
-
-
?
2-methoxy-trans-cinnamate + NH3
2-methoxy-L-phenylalanine
52.7% conversion
-
-
?
3-chloro-trans-cinnamate + NH3
3-chloro-L-phenylalanine
92.6% conversion
-
-
?
3-fluoro-trans-cinnamate + NH3
3-fluoro-L-phenylalanine
91.2% conversion
-
-
?
3-hydroxy-trans-cinnamate + NH3
3-hydroxy-L-phenylalanine
70.6% conversion
-
-
?
3-methoxy-trans-cinnamate + NH3
3-methoxy-L-phenylalanine
85.0% conversion
-
-
?
4-chloro-trans-cinnamate + NH3
4-chloro-L-phenylalanine
91.7% conversion
-
-
?
4-fluoro-trans-cinnamate + NH3
4-fluoro-L-phenylalanine
84.7% conversion
-
-
?
4-hydroxy-trans-cinnamate + NH3
4-hydroxy-L-phenylalanine
0.9% conversion
-
-
?
4-methoxy-trans-cinnamate + NH3
4-methoxy-L-phenylalanine
2.5% conversion
-
-
?
L-tyrosine
trans-p-hydroxycinnamate + NH3
the enzyme is specific for L-phenylalanine, and shows low activity with L-tyrosine
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
the enzyme is involved in phenylpropanoid biosynthesis
-
-
?
2-chloro-trans-cinnamate + NH3
2-chloro-L-phenylalanine
96.4% conversion
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
the enzyme is involved in phenylpropanoid biosynthesis
-
-
?
L-phenylalanine
trans-cinnamate + NH3
the enzyme is specific for L-phenylalanine, and shows low activity with L-tyrosine
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
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
the enzyme is involved in phenylpropanoid biosynthesis
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
the enzyme is involved in phenylpropanoid biosynthesis
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,5-dihydro-5-methylidene-4H-imidazol-4-one
the cofactor is regenerated during the reaction cycle and thus does not require external cofactor regeneration
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
vascular tissue, AtPAL1 and AtPAL2
vascular tissue, AtPAL1 and AtPAL2
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the pal1 pal2 double knockout mutant is almost devoid of flavonoids
metabolism
physiological function
Arabidopsis KFB proteins physically interact with and mediate the proteolytic turnover of four PAL isozymes (PAL1, PAL2, PAL3, PAL4)
malfunction
the pal1 pal2 double knockout mutant is almost devoid of flavonoids
metabolism
physiological function
Arabidopsis KFB proteins physically interact with and mediate the proteolytic turnover of four PAL isozymes (PAL1, PAL2, PAL3, PAL4)
metabolism
AtPAL isogenes differentially respond to environmental stresses and AtPAL1 and AtPAL2 have functional specialization in environmentally triggered phenolic synthesis
metabolism
isogenes AtPAL1, 2, and 4 show close association with lignin biosynthesis
metabolism
the enzyme is involved in phenylpropanoid biosynthesis. The gateway enzyme plays a key role in mediating carbon flux from primary metabolism into the phenylpropanoid pathway
metabolism
AtPAL isogenes differentially respond to environmental stresses and AtPAL1 and AtPAL2 have functional specialization in environmentally triggered phenolic synthesis
metabolism
isogenes AtPAL1, 2, and 4 show close association with lignin biosynthesis
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_ARATH
725
0
78726
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F144H
decrease of activity with L-phenylalanine, increase of activity with L-tyrosine
F144H
-
marked reduction (30fold) in affinity for the substrate phenylalanine
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isogenes AtPAL-1, -2, and -4 have much higher expression levels than AtPAL-3
nitrogen depletion induces the expression of PAL1 and PAL2
isogenes AtPAL-1, -2, and -4 have much higher expression levels than AtPAL-3
nitrogen depletion induces the expression of PAL1 and PAL2
treatment of seedlings with 5 mM 3-aminobenzamide significantly reduces PAL activity in elf18-elicited seedlings
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
transgenic roots of Coleus blumei, harbouring the Arabidopsis thaliana PAL1 gene, under the control of the CaMV 35S promoter, show disparate phenylalanine ammonia-lyase activities ranging from 67 to 350%, compared to wild-type roots. Growth rates significantly differ, with the lowest in transgenic roots exerting augmented phenylalanine ammonia-lyase activity. Transgenic roots with high phenylalanine ammonia-lyase activity have lower growth rates, lower amounts of total phenolics, rosmarinic acid, i.e. the major phenolic compound in Coleus blumei and chlorogenic acid, but increased amounts of caffeic acid. There is no increase in total phenolics and rosmarinic acid content after feeding transgenic roots with casein enzymatic hydrolysate and L-tyrosine
drug development
AtPAL2 is a very good catalyst for the formation of 3-fluoro-L-phenylalanine, 4-fluoro-L-phenylalanine and 2-chloro-L-phenylalanine. Such noncanonical amino acids are valuable building blocks for the formation of various drug molecules
pharmacology
the enzyme is specifically advantageous for the production of the hypertension drug 2-chloro-L-phenylalanine
synthesis
synthesis
AtPAL2 is a very good catalyst for the formation of 3-fluoro-L-phenylalanine, 4-fluoro-L-phenylalanine and 2-chloro-L-phenylalanine. Such noncanonical amino acids are valuable building blocks for the formation of various drug molecules
synthesis
-
reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including trans-cinnamic acid, (2RS)-pinocembrin, styrene, pinosylvin or (2S)-naringenin
synthesis
the enzyme is specifically advantageous for the production of 2-chloro-L-phenylalanine, an important intermediate for the synthesis of angiotensin 1-converting enzyme inhibitors
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cochrane, F.C.; Davin, L.B.; Lewis, N.G.
The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms
Phytochemistry
65
1557-1564
2004
Arabidopsis thaliana (P35510), Arabidopsis thaliana (P45724), Arabidopsis thaliana (P45725), Arabidopsis thaliana (Q9SS45), Arabidopsis thaliana
Watts, K.T.; Mijts, B.N.; Lee, P.C.; Manning, A.J.; Schmidt-Dannert, C.
Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family
Chem. Biol.
13
1317-1326
2006
Arabidopsis thaliana (P35510)
Adams-Phillips, L.; Briggs, A.G.; Bent, A.F.
Disruption of poly(ADP-ribosyl)ation mechanisms alters responses of Arabidopsis to biotic stress
Plant Physiol.
152
267-280
2010
Arabidopsis thaliana
Bauer, N.; Fulgosi, H.; Jelaska, S.
Overexpression of phenylalanine ammonia-lyase in transgenic roots of Coleus blumei alters growth and rosmarinic acid synthesis
Food Technol. Biotechnol.
49
24-31
2011
Arabidopsis thaliana (P35510)
-
Zhang, X.; Gou, M.; Liu, C.J.
Arabidopsis Kelch repeat F-box proteins regulate phenylpropanoid biosynthesis via controlling the turnover of phenylalanine ammonia-lyase
Plant Cell
25
4994-5010
2013
Arabidopsis thaliana (P35510), Arabidopsis thaliana (P45724), Arabidopsis thaliana (P45725), Arabidopsis thaliana (Q9SS45), Arabidopsis thaliana
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
Dressen, A.; Hilberath, T.; Mackfeld, U.; 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 II Application in different reactor concepts for the production of (S)-2-chloro-phenylalanine
J. Biotechnol.
258
158-166
2017
Arabidopsis thaliana (P45724), Arabidopsis thaliana
Zhang, X.; Liu, C.J.
Multifaceted regulations of gateway enzyme phenylalanine ammonia-lyase in the biosynthesis of phenylpropanoids
Mol. Plant
8
17-27
2015
Arabidopsis thaliana (P35510), Arabidopsis thaliana (P45724), Arabidopsis thaliana (P45725), Arabidopsis thaliana (Q9SS45)
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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