Information on EC 4.3.1.24 - phenylalanine ammonia-lyase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
4.3.1.24
-
RECOMMENDED NAME
GeneOntology No.
phenylalanine ammonia-lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-phenylalanine = trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
L-phenylalanine = trans-cinnamate + NH3
show the reaction diagram
E1cb mechanism
-
L-phenylalanine = trans-cinnamate + NH3
show the reaction diagram
analysis of active-site structure analysis and reaction mechanism in which the amino group of the phenylalanine substrate is attacked directly by the 4-methylidene-imidazole-5-one prosthetic group, the reaction proceeds through a carbanion intermediate, Tyr78 acts as a general base, helix-to-loop conformational switch in the helices flanking the inner active-site loop that regulates accessibility of the active site, modeling, overview
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C-N bond formation
Rhodococcus rubra, Rhodotorula mucilaginosa
-
-
PATHWAY
KEGG Link
MetaCyc Link
benzoate biosynthesis II (CoA-independent, non-beta-oxidative)
-
Biosynthesis of secondary metabolites
-
ephedrine biosynthesis
-
Metabolic pathways
-
Phenylalanine metabolism
-
Phenylpropanoid biosynthesis
-
phenylpropanoid biosynthesis, initial reactions
-
suberin monomers biosynthesis
-
trans-cinnamoyl-CoA biosynthesis
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AtPAL 1
P35510
-
AtPAL 2
P45724
-
AtPAL 3
P45725
-
AtPAL 4
Q9SS45
-
EC 4.3.1.5
-
formerly
EC 4.3.1.5
Q6ST23
formerly
EC 4.3.1.5
-
formerly
EC 4.3.1.5
-
formerly
EC 4.3.1.5
-
formerly
EC 4.3.1.5
P52777
formerly
EC 4.3.1.5
Q8VXG7
formerly
L-phenylalanine ammonia-lyase
C6ZIA5, P25872, P35513, P45733
-
L-phenylalanine ammonia-lyase
-
-
L-phenylalanine ammonia-lyase
Rhodotorula aurantiaca KM-1
-
-
-
L-phenylalanine ammonia-lyase
Q2VMT1
-
L-phenylalanine-ammonia lyase
-
-
PAL
D0E576
-
PAL
C0LL35
-
PAL
Q672H7
-
PAL
Camellia sinensis O. Kuntze
-
-
-
PAL
B5LAW0
-
PAL
B5U983
-
PAL
Euphorbia pulcherrima willd.
B9VR52
-
-
PAL
Gossypium hirsutum Zhongmian 35
-
-
-
PAL
-
-
PAL
C6ZIA5
-
PAL
P52777
-
PAL
Rhodotorula aurantiaca KM-1
-
-
-
PAL
Rhodotorula glutinis AS2.102, Rhodotorula glutinis RE4607095D
-
-
-
PAL
Q43210
-
PAL
Q8VXG7
-
PAL1
P35510
gene name
PAL1
Q6ST23
isoform
PAL1
D3Y5L6
gene name
PAL1
B0M0P5
-
PAL1
Q0GA81
-
PAL1
P25872
-
PAL1
A9XIW5
-
PAL2
C0LL35
gene name
PAL2
Q6ST23
gene name
PAL2
P35513
-
PAL3
Q852S1
-
PAL3
P45733
-
PAL4
D5KS97
-
PAL5
P35511
isoform
PAL6
F8RL28
-
PALrs1
Q5EIB6
-
phenylalanine ammonia lyase
-
-
phenylalanine ammonia-lyase
C0LL35
-
phenylalanine ammonia-lyase 1
P35510
-
phenylalanine ammonia-lyase 2
P45724
-
phenylalanine ammonia-lyase 3
P45725
-
phenylalanine ammonia-lyase 4
Q9SS45
-
LsPAL1
-
wound-inducible phenylalanine ammonia-lyase
additional information
B5U983
Ephedra sinica and and Pinus sp. PAL form a gymnosperm-type PAL subfamily
CAS REGISTRY NUMBER
COMMENTARY
9024-28-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Alternaria sp.
2 different enzyme forms are isolated after 68 h and after 116 h: PAL68 and PAL116
-
-
Manually annotated by BRENDA team
strain ATCC 29415
-
-
Manually annotated by BRENDA team
isoform Pal1
SwissPRot
Manually annotated by BRENDA team
PAL1; var. mongholicus, i.e. Astralagus mongholicus, a Chinese traditional medicinal herb, gene PAL1
UniProt
Manually annotated by BRENDA team
; isoform Pal2
UniProt
Manually annotated by BRENDA team
isoform PAL2
UniProt
Manually annotated by BRENDA team
isoform PAL4
UniProt
Manually annotated by BRENDA team
Bovista sp.
weak
-
-
Manually annotated by BRENDA team
var. integrifolia
-
-
Manually annotated by BRENDA team
ssp. napus var. pekinensis
-
-
Manually annotated by BRENDA team
Camellia sinensis O. Kuntze
-
-
-
Manually annotated by BRENDA team
Serrano type strain CM-334
UniProt
Manually annotated by BRENDA team
treatment of plants with Pseudmonas sp. increases shoot length and significantly increases the activity of both peroxidase and phenylalanine ammonia-lyase
-
-
Manually annotated by BRENDA team
isoform PAL1
UniProt
Manually annotated by BRENDA team
infected with Penicillium digitatum
-
-
Manually annotated by BRENDA team
Clavaria cristata
-
-
-
Manually annotated by BRENDA team
cucumber
-
-
Manually annotated by BRENDA team
marrow
-
-
Manually annotated by BRENDA team
gene pal1, fragment; gene pal1
UniProt
Manually annotated by BRENDA team
gene pal2, fragment; gene pal2
UniProt
Manually annotated by BRENDA team
gene pal3a, fragment; gene pal3a
UniProt
Manually annotated by BRENDA team
gene pal3b; gene pal4
-
-
Manually annotated by BRENDA team
at least two active PAL genes, gene DcPAL1 encodes isozyme PAL1
UniProt
Manually annotated by BRENDA team
L. ssp. sativa var. Bangor
-
-
Manually annotated by BRENDA team
PAL3; at least two active PAL genes, gene DcPAL3 encodes isozyme PAL3
UniProt
Manually annotated by BRENDA team
Dunaliella marina
-
-
-
Manually annotated by BRENDA team
PAL1; several pal genes encode at least four isoforms of PAL
UniProt
Manually annotated by BRENDA team
Euphorbia pulcherrima willd.
-
UniProt
Manually annotated by BRENDA team
Fomes subroseus
-
-
-
Manually annotated by BRENDA team
cv. Camarosa and Toyonoka
UniProt
Manually annotated by BRENDA team
cultivar Da jing zhui
-
-
Manually annotated by BRENDA team
gene GbPAL
UniProt
Manually annotated by BRENDA team
Zhongmian 35
-
-
Manually annotated by BRENDA team
Gossypium hirsutum Zhongmian 35
Zhongmian 35
-
-
Manually annotated by BRENDA team
cultivares LM-109 and UNA-80
-
-
Manually annotated by BRENDA team
L. var. Aravat
-
-
Manually annotated by BRENDA team
synonym Ipomoea nil, variants Violet and Tendan
-
-
Manually annotated by BRENDA team
L. var. longifolia
-
-
Manually annotated by BRENDA team
var. Col, romaine lettuce
-
-
Manually annotated by BRENDA team
Lupinus sp.
-
-
-
Manually annotated by BRENDA team
AAA Cavendish. cv. Brazil, banana, isozymes PAL1 and PAL2
-
-
Manually annotated by BRENDA team
cv. Xanthi-nc
-
-
Manually annotated by BRENDA team
isoform PAL1; cultivar Xanthi
UniProt
Manually annotated by BRENDA team
isoform PAL2; cultivar Xanthi
UniProt
Manually annotated by BRENDA team
isoform PAL3; cultivar Xanthi
UniProt
Manually annotated by BRENDA team
isoform PAL4; cultivar Xanthi
UniProt
Manually annotated by BRENDA team
strain ATCC 29133
-
-
Manually annotated by BRENDA team
cultivars Picual, Verdial, Arbequina, and Frantoio
-
-
Manually annotated by BRENDA team
cv. purple puttu
-
-
Manually annotated by BRENDA team
L.cv. Nipponbare
-
-
Manually annotated by BRENDA team
variant crispa
-
-
Manually annotated by BRENDA team
Nym., 4 isoenzymes: PAL 1, PAL 2, PAL 3, PAL 4
-
-
Manually annotated by BRENDA team
recombinant wild-type enzyme and mutant enzymes Q487A, Y350F, and L137H
-
-
Manually annotated by BRENDA team
multiple MW-forms: 83000 Da and 77000 Da
-
-
Manually annotated by BRENDA team
cultivars Telia and Muktateshi
-
-
Manually annotated by BRENDA team
loblolly pine, genotype no. 1932
UniProt
Manually annotated by BRENDA team
Polyporus adustus
-
-
-
Manually annotated by BRENDA team
Quercus pedunculata
-
-
-
Manually annotated by BRENDA team
Ramaria secunda
-
-
-
Manually annotated by BRENDA team
PALrs1; gene PALrs1
UniProt
Manually annotated by BRENDA team
Rhodococcus rubra
Genex 1983
-
-
Manually annotated by BRENDA team
strain KM-1
-
-
Manually annotated by BRENDA team
Rhodotorula aurantiaca KM-1
strain KM-1
-
-
Manually annotated by BRENDA team
Rhodotorula aurantiaca NCYC138
NCYC138
-
-
Manually annotated by BRENDA team
commercial product, 60% v/v solution in glycerol
-
-
Manually annotated by BRENDA team
strain AS2.102
-
-
Manually annotated by BRENDA team
strain RE4607095D
-
-
Manually annotated by BRENDA team
Rhodotorula glutinis AS2.102
strain AS2.102
-
-
Manually annotated by BRENDA team
Rhodotorula glutinis NCYC61
NCYC61
-
-
Manually annotated by BRENDA team
Rhodotorula glutinis RE4607095D
strain RE4607095D
-
-
Manually annotated by BRENDA team
Rhodotorula graminis NCYC502
NCYC502
-
-
Manually annotated by BRENDA team
Rhodotorula marina NCYC541
NCYC541
-
-
Manually annotated by BRENDA team
Rhodotorula minuta PRL155
PRL155
-
-
Manually annotated by BRENDA team
Rhodotorula mucilaginosa PRL251
PRL251
-
-
Manually annotated by BRENDA team
Rhodotorula texensis
-
-
-
Manually annotated by BRENDA team
PAL is encoded by two genes, RiPAL1 and RiPAL2
-
-
Manually annotated by BRENDA team
gene pal1
UniProt
Manually annotated by BRENDA team
cv. Craigella near-isolines, susceptible CSG CR 26 and resistant CRG CR 218 to Verticillium dahliae race 1, multi-gene family with about 26 copies in the diploid genome
UniProt
Manually annotated by BRENDA team
three isozymes
UniProt
Manually annotated by BRENDA team
treatment of plants with Pseudmonas sp. increases shoot length and significantly increases the activity of both peroxidase and phenylalanine ammonia-lyase
-
-
Manually annotated by BRENDA team
2 enzyme forms which are not interconvertible
-
-
Manually annotated by BRENDA team
Sporobolomyces pararoseus
-
-
-
Manually annotated by BRENDA team
Steccherinum adustum
-
-
-
Manually annotated by BRENDA team
Streptomyces verticillatus
-
-
-
Manually annotated by BRENDA team
avr. red spring
UniProt
Manually annotated by BRENDA team
var. Red Spring
-
-
Manually annotated by BRENDA team
Appeldoorn
-
-
Manually annotated by BRENDA team
Tulipa hybrid cultivar Appeldoorn
Appeldoorn
-
-
Manually annotated by BRENDA team
corn smut fungus
-
-
Manually annotated by BRENDA team
wild-growing grape, genes PAL1, PAL2, and PAL3
-
-
Manually annotated by BRENDA team
cv. Cabernet Sauvignon
Uniprot
Manually annotated by BRENDA team
Xanthium pennsylvanicum
-
-
-
Manually annotated by BRENDA team
cultivars Japanese Striped corn and Indian Blue corn
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
C6ZIA5, P25872, P35513, P45733
L-phenylalanine ammonia-lyase is the first enzyme of phenylpropanoid biosynthesis; L-phenylalanine ammonia-lyase is the first enzyme of phenylpropanoid biosynthesis; L-phenylalanine ammonia-lyase is the first enzyme of phenylpropanoid biosynthesis; L-phenylalanine ammonia-lyase is the first enzyme of phenylpropanoid biosynthesis
metabolism
-
PAL is a major marker of phenylpropanoid pathway
physiological function
-
activities of polyphenol oxidase and PAL are highest after cultivation at low day/night temperatures of 20/13C, as is anthocyanin content
physiological function
-
suppression of PAL by RNAi leads to plants exhibiting phenotypes such as stunted growth, delayed root formation, altered leaves, and reduced lignin deposition. The total phenolic content is decreased by 20-70% in PAL-suppressed lines, and is accompanied by lower PAL activity. Down-regulation of PAL also affects the expression of cinnamate 4-hydroxylase, 4-coumarate:coenzyme A ligase2, and tyrosine aminotransferase, related genes in the rosmarinic acid pathway. Rosmarinic acid and salvianolic acid B are markedly reduced in PAL-suppressed lines
physiological function
-
during culture of Morinda citrifolia adventitious roots in different strength, i.e. 0.25, 0.50, 0.75, 1.0, 1.5 and 2.0 of Murashige and Skoog medium supplemented with 5 mg/l indole butyric acid and 30 g/l sucrose, phenylalanine ammonia lyase activity shows a positive correlation in relation to salt strength that leads to an increase in phenol biosynthesis in expense of anthraquinone formation. With the increasing salt strength, root growth and anthraquinone accumulation decrease significantly
physiological function
-
PAL activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 24 hours after inoculation in the resistant varieties. Defense enzymes PAL, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. PAL is induced first, followed by tyrosine ammonia-lyase and than polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
physiological function
Camellia sinensis O. Kuntze
-
PAL activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 24 hours after inoculation in the resistant varieties. Defense enzymes PAL, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. PAL is induced first, followed by tyrosine ammonia-lyase and than polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E)-3-(1-benzofuran-2-yl)acrylic acid + NH3
2-amino-3-(1-benzofuran-2-yl)propanoic acid
show the reaction diagram
-
-
-
-
r
(2E)-3-(1-benzothien-2-yl)acrylic acid + NH3
2-amino-3-(1-benzothien-2-yl)propanoic acid
show the reaction diagram
-
-
-
-
r
(2E)-3-(2-furyl)acrylic acid + NH3
(S)-2-amino-3-(2-furyl)propanoic acid
show the reaction diagram
-
-
-
-
r
(2E)-3-(2-thienyl)acrylic acid + NH3
2-amino-3-(2-thienyl)propanoic acid
show the reaction diagram
-
-
-
-
r
(2E)-4-amino-cinnamic acid + NH3
4-amino-L-phenylalanine
show the reaction diagram
-
poor substrate
-
-
r
(2E)-4-fluoro-cinnamic acid + NH3
4-fluoro-L-phenylalanine
show the reaction diagram
-
-
-
-
r
(2E)-4-formyl-cinnamic acid + NH3
4-formyl-L-phenylalanine
show the reaction diagram
-
-
-
-
r
(2E)-4-hydroxycinnamate + NH3
L-tyrosine
show the reaction diagram
-
-
-
-
r
(2E)-4-methyl-cinnamic acid + NH3
4-methyl-L-phenylalanine
show the reaction diagram
-
-
-
-
r
(2E)-4-nitro-cinnamic acid + NH3
4-nitro-L-phenylalanine
show the reaction diagram
-
-
-
-
r
(2E)-4-trifluoromethyl-cinnamic acid + NH3
4-trifluoromethyl-L-phenylalanine
show the reaction diagram
-
poor substrate
-
-
r
(E)-cinnamate+ NH3
L-phenylalanine
show the reaction diagram
-
-
-
-
r
2,3,4,5,6-pentafluoro-L-phenylalanine
2,3,4,5,6-pentafluoro-trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
2,6-difluoro-L-phenylalanine
2,6-difluoro-trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
2-amino-3-(1-benzofuran-2-yl)propanoic acid
(2E)-3-(1-benzofuran-2-yl)acrylic acid + NH3
show the reaction diagram
-
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
show the reaction diagram
-
14% of the rate with L-phenylalanine
-
-
r
2-amino-3-(2-furyl)propanoic acid
(2E)-3-(2-furyl)acrylic acid + NH3
show the reaction diagram
-
34% of the rate with L-phenylalanine
-
-
r
2-amino-3-(2-thienyl)propanoic acid
(2E)-3-(2-thienyl)acrylic acid + NH3
show the reaction diagram
-
101% of the rate with L-phenylalanine
-
-
r
2-amino-3-(3-thienyl)propanoic acid
(2E)-3-(3-thienyl)acrylic acid + NH3
show the reaction diagram
-
16% of the rate with L-phenylalanine
-
-
r
2-chloro-L-phenylalanine
2-chloro-trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
2-fluoro-L-phenylalanine
2-fluoro-trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
3,4-dihydroxyphenylalanine
?
show the reaction diagram
-
29% of the activity with L-Phe
-
-
?
3,5-difluoro-L-phenylalanine
3,5-difluoro-trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
3-chloro-L-phenylalanine
3-chloro-trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
3-fluoro-L-phenylalanine
3-fluoro-trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
4-chloro-L-phenylalanine
4-chloro-trans-cinnamate + NH3
show the reaction diagram
-
-
-
?
4-fluoro-L-phenylalanine
4-fluoro-trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
4-fluoro-L-phenylalanine
4-fluoro-(E)-cinnamate + NH3
show the reaction diagram
-
-
-
-
r
4-nitro-L-phenylalanine
4-nitro-(E)-cinnamate + NH3
show the reaction diagram
-
-
-
-
r
4-trifluoromethyl-L-phenylalanine
4-trifluoromethyl-(E)-cinnamate + NH3
show the reaction diagram
-
-
-
-
r
beta-(5-pyrimidinyl)-D,L-alanine
?
show the reaction diagram
-
-
-
?
chlorophenylalanine
?
show the reaction diagram
Streptomyces verticillatus
-
-
-
-
?
fluorophenylalanine
trans-(4-fluoro)cinnamate + NH3
show the reaction diagram
Streptomyces verticillatus
-
-
-
-
?
fluorophenylalanine
trans-(4-fluoro)cinnamate + NH3
show the reaction diagram
-
p-fluorophenylalanine, 31% of the activity with L-Phe, o-fluorophenylalanine, 14% of the activity with L-Phe
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
Lupinus sp.
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
Streptomyces verticillatus
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
Streptomyces verticillatus
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
Rhodotorula texensis, Sporobolomyces roseus
-
-
-
?
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
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
Quercus pedunculata
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
Alternaria sp.
-
-
-
-
?
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
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
Bovista sp., Clavaria cristata, Fomes subroseus, Phlebia tremellosa, Polyporus adustus, Ramaria secunda, Steccherinum adustum, Tricladium splendens
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
P35510, P45724, P45725, Q9SS45
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-, C0LL35, D5KS97
-
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
no activity with D-Phe
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
cutting induces phenylalanine ammonia-lyase
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
the enzyme catalyzes the first step controlling the rate of phenylpropanoid metabolism, wound-inducible enzyme
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
P11544
mechanism: multiple helix dipoles implicated in catalysis
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
Tulipa hybrid cultivar Appeldoorn
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
show the reaction diagram
-, C0LL35, D5KS97
-
-
-
?
L-Phe
(E)-cinnamate + NH3
show the reaction diagram
-, Q0GA81
-
-
-
?
L-Phe
(E)-cinnamate + NH3
show the reaction diagram
D3Y5L6
-
-
-
?
L-Phe
trans-cinnamic acid + NH3
show the reaction diagram
C0LL35
-
-
-
?
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
-
-
-
-
?
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
-
-
-
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
-
-
-
-
r
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
?, r
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
C0LL35
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
P45735
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
P35511
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-, Q52QH3
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
B0M0P5, Q852S1
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
P11544
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
A9XIW5
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
B1GS29, B1GS31, B1GS33, -
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Q5EIB6, -
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Q2VMT1
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
B5LAW0
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Q43210
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
A7UHB6
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
B5U983, -
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Q672H7
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-, Q6ST23
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
C6ZIA5, P25872, P35513, P45733
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
P52777
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Q8VXG7, -
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
D0E576
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
reaction can be reversed by applying high concentrations of ammonia
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
first enzyme in the phenylpropanoid biosynthetic pathway
-
r
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
B5LAW0
a key enzyme in the synthesis of phenolic compounds, including phytoalexins, with anti-microbial antimicrobial properties that are important in the defence of plants
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
A7UHB6
first step in flavonoid biosynthesis, the enzyme might have a regulatory role in flavonoid biosynthesis at transcriptional level
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Q672H7
first step in phenylpropanoid and flavonoid biosynthesis pathways, overview
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
B5U983, -
in ephedrine alkaloid biosynthesis in Ephedra, trans-cinnamic acid produced from a PAL reaction is converted into benzoic acid or benzoyl-CoA by beta-oxidation, branching off from the common phenylpropanoid pathway, biosynthetic pathway of ephedrine alkaloids, overview
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
P45735
key enzyme in phenylpropanoid metabolism of grape berry
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Q43210
PAL is a key enzyme in plant stress responses
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
P35511
phenylalanine ammonia-lyase is an important enzyme in both plant development and pathogen defense
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
phenylalanine ammonia-lyase is the first enzyme in the phenylpropanoid pathway catalyzing monooxidative deamination of phenylalanine to produce cinnamate, overview
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
B0M0P5, Q852S1
regulatory mechanism on PAL gene expression, overview
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-, Q52QH3
the enzyme catalyzes the first step in the biosynthetic pathway leading to calycosin-7-O-beta-D-glucoside, overview. Accumulation of mRNA for calycosin-7-O-beta-Dglucoside pathway genes during different temperature treatments
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Q5EIB6, -
the enzyme is involved in the biosynthesis of salidroside, an effective adaptogenic drug extracted from the medicinal plant Rhodiola sachalinensis, two different possible biosynthetic pathways via tyrosol, overview
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
the enzyme is involved in the plant's defense system
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
the enzyme is part of the plant's defense system, especially in the early stages of seed maturation
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
A9XIW5
Ala-Ser-Gly triad
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
the enzyme catalyzes the reverse reaction from a 2% trans-cinnamic acid with (NH4)2SO4 solution
-
-
r
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
assay at 40C, pH 7.8
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Rhodotorula glutinis RE4607095D
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Rhodotorula glutinis AS2.102
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Rhodotorula glutinis AS2.102
-
the enzyme catalyzes the reverse reaction from a 2% trans-cinnamic acid with (NH4)2SO4 solution
-
-
r
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Rhodotorula aurantiaca KM-1
-
-
-
-
?
L-phenylalanine
trans-cinnamate
show the reaction diagram
-
-
-
?
L-phenylalanine
trans-cinnamic acid + NH3
show the reaction diagram
C0LL35
assay at pH 8.5, 37C, reaction terminated by addition of HCl
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
show the reaction diagram
-
-
-
-
r
L-Tyr
(2E)-4-hydroxycinnamate + NH3
show the reaction diagram
-, Q0GA81
-
-
-
?
L-Tyr
(2E)-4-hydroxycinnamate + NH3
show the reaction diagram
-, C0LL35, D5KS97
poor substrate
-
-
?
L-Tyr
p-coumarate + NH3
show the reaction diagram
-, C0LL35, 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
-
no activity
-
-
-
L-tyrosine
p-coumarate + NH3
show the reaction diagram
-
no activity
-
-
-
L-tyrosine
p-coumarate + NH3
show the reaction diagram
-
no activity
-
-
-
L-tyrosine
p-coumarate + NH3
show the reaction diagram
Streptomyces verticillatus, Ustilago hordei, Pteridium aquilinum
-
no activity
-
-
-
L-tyrosine
p-coumarate + NH3
show the reaction diagram
-
poor substrate
-
-
?
L-tyrosine
p-coumarate + NH3
show the reaction diagram
-
L-Tyr
-
-
-
L-tyrosine
p-coumarate + NH3
show the reaction diagram
-
no deamination of L-Tyr
-
-
-
L-tyrosine
p-coumarate + NH3
show the reaction diagram
-
m-Tyr, 10% of the activity with L-Phe, L-Tyr, 15% of the activity with L-Phe
-
-
?
N-methyl-L-phenylalanine
trans-cinnamate + methylamine
show the reaction diagram
-
-
-
?
trans-cinnamic acid + NH3
L-phenylalanine
show the reaction diagram
Rhodotorula mucilaginosa, Rhodococcus rubra
-
-
-
-
-
L-tyrosine
(2E)-4-hydroxycinnamate + NH3
show the reaction diagram
-
poor substrate
-
-
r
additional information
?
-
-
key enzyme of phenylpropanoid metabolism
-
-
-
additional information
?
-
-
the enzyme is involved in the lignification of pine suspension cultures in response to an elicitor prepared from an extomycorrhizal fungus
-
-
-
additional information
?
-
-
the 83000 Da enzyme form may be constitutive and involved in the low-level accumulation of phenolics in most cell types, the 77000 Da enzyme form is rapidly induced during elicitor action, wounding or cytokinin-induced xylogenesis as a key regulatory enzyme involved in the synthesis of phenolics under stress conditions or during differentiation
-
-
-
additional information
?
-
Alternaria sp.
-
key enzyme in the formation of a variety of phenolic compounds
-
-
-
additional information
?
-
-
UV-B light induces a single PAL isoform, which plays an important role in the regulation of the biosynthesis of phenylpropanoid metabolites
-
-
-
additional information
?
-
-
first enzyme in phenylpropanoid biosynthesis
-
-
-
additional information
?
-
-
first enzyme in phenylpropanoid biosynthesis
-
-
-
additional information
?
-
-
3 isoforms, which are differentially induced and affected by metabolites belonging to particular branches of phenylpropanoid pathway
-
-
-
additional information
?
-
-
enzyme may be involved in detoxification of Cd2+
-
-
-
additional information
?
-
-
no substrate: 2-amino-3-(3-furyl)propanoic acid. Enzyme acts selectively on L-amino acids and their derivatives
-
-
-
additional information
?
-
-
no substrate: L-histidine
-
-
-
additional information
?
-
P35511
PAL activity seems to be extraordinarily sensitive to the physiological state of the plant
-
-
-
additional information
?
-
-, Q52QH3
phenylalanine ammonia lyase PAL1 functions as a switch directly controlling the accumulation of calycosin and calycosin-7-O-beta-D-glucoside in Astragalus membranaceus var. mongholicus plants by limiting the compound levels in a light-dependent manner during low temperature treatment, overview
-
-
-
additional information
?
-
Q672H7
the core reactions of phenylpropanoid metabolism involve three enzymes, phenylalanine ammonia-lyase, cinnamate 4-hydroxylase, and 4-coumarate coenzyme A ligase, pathway, overview
-
-
-
additional information
?
-
-
structure-function relationship, with helix-loop conformational switch, overview
-
-
-
additional information
?
-
C0LL35
L-Tyr is a poor substrate
-
-
-
additional information
?
-
-, C0LL35, D5KS97
no substrate: L-Tyr
-
-
-
additional information
?
-
D3Y5L6
no substrate: L-Tyr
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
cutting induces phenylalanine ammonia-lyase
-
-
?
L-Phe
trans-cinnamate + NH3
show the reaction diagram
-
the enzyme catalyzes the first step controlling the rate of phenylpropanoid metabolism, wound-inducible enzyme
-
-
?
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
-
-
-
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
-
-
-
-
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
-
-
-
r
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
-
-
-
-
?
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
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
P35511
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
P11544
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
A9XIW5
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
B1GS29, B1GS31, B1GS33, -
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Q2VMT1
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
P52777
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
first enzyme in the phenylpropanoid biosynthetic pathway
-
r
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
B5LAW0
a key enzyme in the synthesis of phenolic compounds, including phytoalexins, with anti-microbial antimicrobial properties that are important in the defence of plants
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
A7UHB6
first step in flavonoid biosynthesis, the enzyme might have a regulatory role in flavonoid biosynthesis at transcriptional level
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Q672H7
first step in phenylpropanoid and flavonoid biosynthesis pathways, overview
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
B5U983, -
in ephedrine alkaloid biosynthesis in Ephedra, trans-cinnamic acid produced from a PAL reaction is converted into benzoic acid or benzoyl-CoA by beta-oxidation, branching off from the common phenylpropanoid pathway, biosynthetic pathway of ephedrine alkaloids, overview
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
P45735
key enzyme in phenylpropanoid metabolism of grape berry
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Q43210
PAL is a key enzyme in plant stress responses
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
P35511
phenylalanine ammonia-lyase is an important enzyme in both plant development and pathogen defense
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
phenylalanine ammonia-lyase is the first enzyme in the phenylpropanoid pathway catalyzing monooxidative deamination of phenylalanine to produce cinnamate, overview
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
B0M0P5, Q852S1
regulatory mechanism on PAL gene expression, overview
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-, Q52QH3
the enzyme catalyzes the first step in the biosynthetic pathway leading to calycosin-7-O-beta-D-glucoside, overview. Accumulation of mRNA for calycosin-7-O-beta-Dglucoside pathway genes during different temperature treatments
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Q5EIB6, -
the enzyme is involved in the biosynthesis of salidroside, an effective adaptogenic drug extracted from the medicinal plant Rhodiola sachalinensis, two different possible biosynthetic pathways via tyrosol, overview
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
the enzyme is involved in the plant's defense system
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
the enzyme is part of the plant's defense system, especially in the early stages of seed maturation
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Rhodotorula glutinis RE4607095D
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Rhodotorula glutinis AS2.102
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
Rhodotorula aurantiaca KM-1
-
-
-
-
?
additional information
?
-
-
key enzyme of phenylpropanoid metabolism
-
-
-
additional information
?
-
-
the enzyme is involved in the lignification of pine suspension cultures in response to an elicitor prepared from an extomycorrhizal fungus
-
-
-
additional information
?
-
-
the 83000 Da enzyme form may be constitutive and involved in the low-level accumulation of phenolics in most cell types, the 77000 Da enzyme form is rapidly induced during elicitor action, wounding or cytokinin-induced xylogenesis as a key regulatory enzyme involved in the synthesis of phenolics under stress conditions or during differentiation
-
-
-
additional information
?
-
Alternaria sp.
-
key enzyme in the formation of a variety of phenolic compounds
-
-
-
additional information
?
-
-
UV-B light induces a single PAL isoform, which plays an important role in the regulation of the biosynthesis of phenylpropanoid metabolites
-
-
-
additional information
?
-
-
first enzyme in phenylpropanoid biosynthesis
-
-
-
additional information
?
-
-
first enzyme in phenylpropanoid biosynthesis
-
-
-
additional information
?
-
-
3 isoforms, which are differentially induced and affected by metabolites belonging to particular branches of phenylpropanoid pathway
-
-
-
additional information
?
-
-
enzyme may be involved in detoxification of Cd2+
-
-
-
additional information
?
-
P35511
PAL activity seems to be extraordinarily sensitive to the physiological state of the plant
-
-
-
additional information
?
-
-, Q52QH3
phenylalanine ammonia lyase PAL1 functions as a switch directly controlling the accumulation of calycosin and calycosin-7-O-beta-D-glucoside in Astragalus membranaceus var. mongholicus plants by limiting the compound levels in a light-dependent manner during low temperature treatment, overview
-
-
-
additional information
?
-
Q672H7
the core reactions of phenylpropanoid metabolism involve three enzymes, phenylalanine ammonia-lyase, cinnamate 4-hydroxylase, and 4-coumarate coenzyme A ligase, pathway, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3,5-dihydro-5-methylidene-4H-imidazol-4-one
P24481
MIO cofactor
3,5-dihydro-5-methylidene-4H-imidazol-4-one
-
MIO cofactor
3,5-dihydro-5-methylidene-4H-imidazol-4-one
Q43210
prosthetic group
4-methylidene-imidazole-5-one
-
deamination of L-Phe is dependent upon a 4-methylidene-imidazole-5-one prosthetic group that is produced by the posttranslational condensation of a sequential Ala-Ser-Gly triad in the enzyme
additional information
C0LL35
PAL2 sequence containes a conserved active site motif, the Ala-Ser-Gly triad, which can be converted into a 3,5-dihydro-5-methylidine-4H-imidazol-4-one prosthetic group
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
partially stabilizes the enzyme during storage, but less effective than Mn2+
Cd2+
-
treatment of roots leads to increase in mRNA level and in enzyme activity. The increase in activity is not directly correlated with the increase in mRNA
Cd2+
-
treatment of roots leads to decrease in mRNA level and increase in enzyme activity
Cs+
D3Y5L6
1 mM, weak enhancement
Li+
-
partially stabilizes the enzyme during storage, but less effective than Mn2+
Mg2+
-
approx. 3fold activation at 8 mM
Mg2+
-
stabilizes the enzyme during storage, but slightly less effective than Mn2+
Mn2+
-
approx. 1.5fold activation at 8 mM
Mn2+
-
stabilizes the enzyme during storage, overview
Ni2+
-
induces the enzyme in cotyledons, highest activity at 0.40 mM nickel, overview
Pb2+
-
treatment of roots leads to increase in mRNA level and in enzyme activity. The increase in activity is not directly correlated with the increase in mRNA
Zn2+
-
partially stabilizes the enzyme during storage, but less effective than Mn2+
Mn2+
D3Y5L6
1 mM, weak enhancement
additional information
-
no requirement for metal ion cofactors
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(+)-1-amino-3',4'-dichlorobenzylphosphonic acid
-
strongest inhibitor among 1-aminobenzylphosphonic acids
(+-)-2-aminomethyl-3-phenylpropanoic acid
-
-
(+-)-2-aminooxy-3-phenylpropanoic acid
-
strong inhibition
(2S)-2-amino-3-(1-benzofuran-3-yl)propanoic acid
-
competitive
(2S)-2-amino-3-(1-benzothien-3-yl)propanoic acid
-
competitive
(R)-1-amino-2-(4-fluorophenyl)ethylphosphonic acid
-
-
(R)-1-amino-2-phenylwthylphosphonic acid
-
strong inhibition
(S)-2-aminooxy-3-phenylpropanoic acid
-
-
(S)-2-aminooxy-3-phenylpropanoic acid
-
very strong inhibition
1-amino-2-phenylethyl-phosphonic acid
-
(R)-1-amino-2-phenylethyl-phosphonic acid
1-amino-2-phenylethyl-phosphonic acid
-
-
1-amino-3-phenylpropylphosphonate
-
inhibitory effect is half of that of 1-amino-2-phenylethyl-phosphonic acid
1-aminobenzylphosphonic acid
-
various substitutes in the benzene ring
2-amino-3-(1-benzofuran-3-yl)propanoic acid
-
competitive
2-amino-3-(1-benzothien-3-yl)propanoic acid
-
competitive
2-amino-4-bromoindane-2-phosphonic acid
-
-
2-amino-4-hydroxyindane-2-phosphonic acid
-
-
2-aminoindan-2-carboxylic acid
-
-
2-aminoindan-2-phosphonic acid
-
-
2-aminoindan-2-phosphonic acid
-
-
2-aminoindan-2-phosphonic acid
-
-
2-aminoindan-2-phosphonic acid
-
strongly inhibits PAL activity, such that PAL activity is reduced to about 48.2% of the control level at 9 days of storage at 8C
2-aminoindan-2-phosphonic acid
D3Y5L6
competitive, specific inhibitor
2-aminoindane-2-phosphonate
-
-
2-aminoindane-2-phosphonate
-
-
2-aminoindane-2-phosphonate
-
-
2-aminoindane-2-phosphonic acid
-
inhibition of browning reaction of cut lettuce at 0.01 mM
2-aminoindane-2-phosphonic acid
-
-
2-mercaptoethanol
-
slight
2-mercaptoethanol
-
above 25 mM
2-mercaptoethanol
C6ZIA5, P25872, P35513, P45733
competitive inhibition; competitive inhibition; competitive inhibition; competitive inhibition
2-methoxy-cinnamaldehyde
-
0.010 mg/ml, 82% inhibition; 0.010 mg/ml, complete inhibition
2-phenyl-4,4,5,5-tetramethyl-imidazoline-1-oxyl-3-oxide
-
partially blocks PAL activity in immobilized cells
3,4-dihydroxybenzoate
-
-
3,4-dihydroxycinnamic acid
-
-
3,4-dihydroxyphenyl-DL-Ala
-
-
3-phenylpropionaldehyde
-
0.010 mg/ml, 67% inhibition
4-coumarate
-
trans-p-coumarate, competitive
4-coumarate
-
-
4-coumarate
Alternaria sp.
-
inhibition of enzyme form PAL116, no inhibition of enzyme form PAL68
4-coumarate
-
-
4-coumarate
-
0.1 mM, slight
4-coumarate
Sporobolomyces pararoseus
-
-
4-hydroxy-3-methoxycinnamic acid
-
-
4-hydroxycinnamic acid
-
-
8-hydroxyquinoline
-
-
ADP
-
5 mM, approx. 50% inhibition
Aminooxyacetate
-
-
aminooxyacetic acid
-
irreversible inhibition, treatment results in decrease in content of 2-hydroxy-4-methoxybenzaldehyde
aminooxyacetic acid
-
-
aminooxyacetic acid
-
a reduction in PAL activity is observed in hairy roots, supplemented with 0.5-1 mM aminooxyacetic acid
aminooxyacetic acid
-
-
aminooxyacetic acid
-
-
AMP
-
5 mM, approx. 40% inhibition
ATP
-
5 mM, approx. 80% inhibition
Benzoate
Alternaria sp.
-
uncompetitive inhibition of enzyme form PAL68, non-competitive inhibition of enzyme form PAL116
benzyl alcohol
-
-
beta-(2-pyrimidinyl)-D,L-alanine
-
competitive inhibition
beta-chloroethyltrimethylammonium
-
10 mM, 60% inhibition of PAL activity in cotyledons
beta-phenyl-DL-Ser
-
-
beta-phenylethylamine
-
-
Ca2+
-
CaCl2, 1 mM, 57% inhibition
Ca2+
-
1 mM, 20% inhibition
Ca2+
-
6 mM, 40% inhibition
caffeate
-
-
caffeate
-
0.1 mM, slight
Cd2+
-
CdCl2, 1 mM, 100% inhibition
chlorogenic acid
-
weak
chlorogenic acid
D3Y5L6
uncompetitive
Cinnamic acid
-
trans-cinnamic acid
Cinnamic acid
Alternaria sp.
-
enzyme form PAL116 is inhibited, no inhibition of enzyme form PAL68
Cinnamic acid
-
competitive; trans-cinnamic acid
Cinnamic acid
-
-
Cinnamic acid
-
-
Cinnamic acid
-
0.1 mM, slight
Cinnamic acid
Sporobolomyces pararoseus
-
-
Cinnamic acid
-
trans-cinnamate, moderately; trans-cinnamic acid
Cinnamic acid
-
trans-cinnamate does not inhibit
Cinnamic acid
-
-
Cinnamic acid
-
(E)-cinnamate, competitive
Cinnamic acid
D3Y5L6
mixed type
Cinnamonitrile
-
-
cinnamyl alcohol
-
-
cinnamyl alcohol
D3Y5L6
uncompetitive
CN-
-
KCN, 1 mM, 85% inhibition
CN-
-
irreversible
CN-
-
irreversible; NaCN
coniferyl alcohol
D3Y5L6
competitive
coniferyl aldehyde
D3Y5L6
competitive
coumaric acid
D3Y5L6
uncompetitive
coumestrol
-
weak
Cu2+
-
CuSO4, 1 mM, 18% inactivation
Cu2+
-
1 mM, 33% inactivation
cyclomaltoheptaose
-
-
cyclomaltohexaose
-
-
D-phenylalanine
-
competitive inhibition
D-phenylalanine
Q2VMT1
competitive inhibition
daidzein
-
weak
dihydrocaffeic acid
-
-
dithiothreitol
-
slight
EDTA
-
35 mM, complete inactivation
ferulate
-
-
fluorophenylalanine
Avena sativa, Ipomoea batatas, Streptomyces verticillatus
-
-
formonetin
-
weak
Gallic acid
-
mixed inhibition
Gallic acid
-
-
genistein
-
weak
genistin
-
weak
heptakis(2,3,6-tri-O-methyl)cyclomaltoheptaose
-
-
-
heptakis(2,3-di-O-methyl)cyclomaltoheptaose
-
competitive and noncompetitive inhibition
-
hexakis(2,3,6-tri-O-methyl)cyclomaltohexaose
-
-
-
hexakis(2,3-di-O-methyl)cyclomaltohexaose
-
competitive and noncompetitive inhibition, activation at 2 and 3 mM
-
Hg2+
-
HgCl2, 0.01 mM, 100% inhibition
Hg2+
D3Y5L6
1 mM, 65% loss of activity
His
Streptomyces verticillatus
-
-
indole butyric acid
Q8VXG7, -
at concentrations higher than 0.001 mM there is inhibitory effect on PAL specific activity
iodoacetamide
-
-
kaempferol
-
mixed inhibition
L-2-aminooxy-3-phenylpropionic acid
-
-
L-alpha-aminooxy-beta-phenylpropionic acid
-, Q52QH3
-
L-alpha-aminooxy-beta-phenylpropionic acid
-
-
N,N-Dicyclohexylcarbodiimide
-
10 mM, 82% inhibition
N,N-dimethyl-4-nitro-L-phenylalanine
-
-
N-acetylimidazol
-
10 mM, 75% inhibition
N-methyl-4-nitro-L-phenylalanine
-
-
NaBH4
-
irreversible
NaBH4
-
irreversible
NaHSO3
-
irreversible
Naringenin
-
-
Nomega-Nitro-L-arginine
-
partially blocks PAL activity in immobilized cells
o-coumarate
-
-
o-coumarate
-
competitive
o-hydroxy-trans-cinnamic acid
-
-
o-phenanthroline
-
20 mM, complete inactivation
p-chloromercuribenzoate
-
slight
p-chloromercuribenzoate
-
-
p-Chloromercuriphenylsulfonic acid
-
-
p-hydroxybenzoate
Alternaria sp.
-
inhibition of enzyme form PAL116, no inhibition of enzyme form P68
p-hydroxybenzoate
-
-
Pb2+
D3Y5L6
1 mM, 50% loss of activity
Phenylmethylsulphonyl fluoride
-
10 mM, 59% inhibition
phenylpropiolic acid
-
-
phenylpyruvate
-
-
quercetin
-
mixed inhibition
quercetin
-
-
salicylic acid
-
PAL activity decreases with prolonged exposure to 0.25 mM salicylic acid indicating its inhibition
salidroside
D3Y5L6
competitive
scopoletin
-
increases the negative cooperativity between the substrate binding sites
Sinapic acid
-
weak
trans-cinnamaldehyde
-
0.010 mg/ml, complete inhibition
trans-Cinnamic acid
-
product inhibition, PAL is tightly regulated by a feedback mechanism
Tyr
-
competitive; L-Tyr
umbelliferone
-
increases the negative cooperativity between the substrate binding sites
Zn2+
-
ZnSO4, 1 mM, 32% inhibition
Zn2+
-
1 mM, complete inhibition
Zn2+
D3Y5L6
1 mM, 65% loss of activity
additional information
-
putative non-diffusible inhibitor
-
additional information
Q672H7
the plant hormones abscisic acid and gibberellic acid GA3 or drought stress lead to downregulation of PAL within several days
-
additional information
B5LAW0
infections with pathogen Nacobbus aberrans alone or in combination with Phytophthora capsici suppress the enzyme expression in strain CM-334 leading to a reduction of enzyme activity by 48% after 21 days, overview
-
additional information
B0M0P5, Q852S1
DcPAL3 promoter activity is strongly repressed by 2,4-dichlorophenoxyacetic acid
-
additional information
-
heat-shock treatment with chlorinated water and ascorbic acid, or with chlorinated water and CaCl2 reduces the enzyme activity, stronger reduction with the latter variant, effects of timing of the treatment before or immediately after cutting, overview
-
additional information
-
cyclodextrins show mixed inhibition, both competitive and noncompetitive, but they also act as activators for selected concentrations. The inhibitory effect of cyclodextrins is connected with the decrease of substrate concentration and unfavourable influence on the flexibility of the enzyme molecules. On the other hand, the activating effect is connected with the decrease of product concentration i.e. the product is an inhibitor of the enzymatic reaction under investigation
-
additional information
D3Y5L6
not inhbitory: tyrosol, caffeic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
2-mercaptoethanol
Q2VMT1
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
abscisic acid
-
exogenous application of abscisic acid (up to 0.08 mM) enhances PAL activity
acetone
P11544
9.0fold
ascorbic acid
-
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
ascorbic acid
Q2VMT1
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
caffeate
-
strong activation
caffeate
-
strong activation
Cd2+
-
treatment with Cd2+ results in increase in enzyme activitiy along with increase in total phenolics content and decrease in content of chlorophyll and carotinoids in the fronds
cetyl trimethyl ammonium bromide
P11544
8.2fold
chitosan
-
treatment leads to increased enzymic activity in cortex and cork tissues, with maximum specific activity after 12 h, and accumulation of phenolic compounds including 2-hydroxy-4-methoxybenzaldehyde
EDTA
-
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
EDTA
Q2VMT1
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
Esculetin
-
activates
fluridone
-
effective in increase of PAL activity
fraxetin
-
activates
jasmonic acid
-
jasmonic acid addition enhances PAL activity
L-phenylalanine
-
exposure of 4-week old plants to phenylalanine increases enzyme activity as well as accumulation of coumarin-related compounds
NaCl
-
maximal activity at 200 mM, inhibition above
phytotoxic protein
-
phytotoxic protein PcF from Phytophthora cactorum induces PAL activity in seedlings
-
S-methyl 1,2,3-benzothiadiazole-7-carbothioate
-
treatment of fruits
salicylic acid
P45735
activates phenylalanine ammonia-lyase in grape berry in response to high temperature stress, it also induces the accumulation of PAL mRNA and the synthesis of new PAL protein, in addition to increasing the enzyme activity, under high temperature stress
scoparone
-
activates
L-tyrosine
-
exposure of 4-week old plants to L-tyrosine at 0.01 or 0.1 mM significantly increases enzyme activity and increases free tyrosine content, while free phenylalanine content decreases. Tyrosine has no effect on coumarin accumulation
additional information
-
treatment of plants with Pseudomonas fluorescens and Pseudomonas aeruginosa induces enzyme synthesis associated with increased synthesis of phenolic compounds such as tannic, gallic, caffeic, chlorogenic and cinnamic acids. Treatment with Sclerotinia slerotiorum does not induce enzyme synthesis
-
additional information
A7UHB6
the enzyme is induced by various stresses, e.g. by UV-B light, wounding, cold, and salicylic acid
-
additional information
-
infection with Bemisia tabaci strongly induces the enzyme in cucumber with a first high activity peak by 23.1% at 6 h after infection and the highest activitypeak by 29.1% at 48 h after infection compared to the control
-
additional information
-
PAL1 and PAL2 are upregulated 1.3-3.8fold in transgenic cells expressing recombinant plant oncogene rolB of Agrobacterium rhizogenes, overview
-
additional information
-, Q52QH3
accumulation of mRNA for calycosin-7-O-beta-D-glucoside pathway genes during different temperature treatments
-
additional information
B0M0P5, Q852S1
transcriptional activation by binding of DcERF1, but not by DcERF2. The trans-activating factors DcERF1 and DcERF2, ethylene-responsive element-binding factors, to the GCC-box homolog sequence, specifically interact with the promoter region, binding specificity, overview. DcERF2 can function as a transcriptional activator when it is localized in the nucleus of carrot protoplasts; transcriptional activation by binding of DcERF1, but not by DcERF2. The trans-activating factors DcERF1 and DcERF2, ethylene-responsive element-binding factors, to the GCC-box homolog sequence, specifically interact with the promoter region, binding specificity, overview. The full DcPAL3 promoter abolishes the upregulation ability of DcERF1. DcERF2 can function as a transcriptional activator when it is localized in the nucleus of carrot protoplasts
-
additional information
Q43210
the enzyme expression is incuced by diverse factors, including pathogenic attack, tissue wounding and UV irradiation, and low temperature
-
additional information
P11544
induction by the combination of L-phenylalanine and L-tyrosine, Ethanol, isopropyl alcohol and chloroform fail to enhance PAL activity significantly
-
additional information
-
heat treatment at 38C for 3 days induces accumulation of PAL protein
-
additional information
P35511
red light, acting via phytochrome, stimulates phenylalanine ammonia lyase activity in cotyledons and hypocotyls of tomato seedlings in a manner dependent on de novo synthesis of protein and nucleic acid. Photostimulation of PAL activity likely requires dephosphorylation by a type 2C protein phosphatase, thus inhibition of protein phosphatase activity blocks increase in PAL activity without affecting the increase in PAL protein levels
-
additional information
-
the enzyme activity is stimulated by chilling, wounding, UV-B light, ozone, pathogen invasion, and plant hormones
-
additional information
Q8VXG7, -
at low concentrations of indole butyric acid (0.0001 and 0.001 mM), there is no significant stimulatory effect on PAL specific activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.3
-
(2E)-4-fluoro-cinnamic acid
-
wild-type, pH 10, 30C
-
0.7
-
(2E)-4-fluoro-cinnamic acid
-
mutant F137V, pH 10, 30C
-
0.1
-
(2E)-4-formyl-cinnamic acid
-
mutant F137V, pH 10, 30C
-
0.4
-
(2E)-4-formyl-cinnamic acid
-
wild-type, pH 10, 30C
-
5.9
-
(2E)-4-hydroxycinnamate
-
mutant F137V, pH 10, 30C
-
12.6
-
(2E)-4-hydroxycinnamate
-
wild-type, pH 10, 30C
-
0.1
-
(2E)-4-methyl-cinnamic acid
-
mutant F137V, pH 10, 30C
-
0.5
-
(2E)-4-methyl-cinnamic acid
-
wild-type, pH 10, 30C
-
2.8
-
(2E)-4-nitro-cinnamic acid
-
wild-type, pH 10, 30C
4.2
-
(2E)-4-nitro-cinnamic acid
-
mutant F137V, pH 10, 30C
0.2
-
(E)-cinnamate
-
mutant F137V, pH 10, 30C; wild-type, pH 10, 30C
0.076
-
2,3,4,5,6-pentafluoro-L-phenylalanine
-
-
0.085
-
2,6-difluoro-L-phenylalanine
-
-
0.048
-
2-amino-3-(1-benzofuran-2-yl)propanoic acid
-
pH 8.8, 30C
0.116
-
2-amino-3-(1-benzothien-2-yl)propanoic acid
-
pH 8.8, 30C
0.076
-
2-amino-3-(2-furyl)propanoic acid
-
pH 8.8, 30C
0.134
-
2-amino-3-(2-thienyl)propanoic acid
-
pH 8.8, 30C
0.018
-
2-amino-3-(3-thienyl)propanoic acid
-
pH 8.8, 30C
0.05
-
2-chloro-L-phenylalanine
-
-
0.065
-
2-fluoro-L-phenylalanine
-
-
0.159
-
3,5-difluoro-L-phenylalanine
-
-
0.094
-
3-chloro-L-phenylalanine
-
-
0.079
-
3-fluoro-L-phenylalanine
-
-
0.045
-
4-chloro-L-phenylalanine
-
-
0.01
-
4-fluoro-L-phenylalanine
-
-
0.4
-
4-fluoro-L-phenylalanine
-
mutant F137V, pH 10, 30C; wild-type, pH 10, 30C
2
-
4-nitro-L-phenylalanine
-
wild-type, pH 10, 30C
2.2
-
4-nitro-L-phenylalanine
-
mutant F137V, pH 10, 30C
2.5
-
4-trifluoromethyl-L-phenylalanine
-
mutant F137V, pH 10, 30C
3.1
-
4-trifluoromethyl-L-phenylalanine
-
wild-type, pH 10, 30C
0.0065
-
L-Phe
-
at low substrate concentrations
0.011
-
L-Phe
-
at low substrate concentrations
0.011
-
L-Phe
-
two different Km-values: 0.011 mM and 0.055 mM
0.015
-
L-Phe
-
isoenzyme PAL-4
0.016
-
L-Phe
-
at high substrate concentrations
0.0169
-
L-Phe
-
isoenzyme PAL-2
0.0172
-
L-Phe
-
isoenzyme PAL-1
0.023
-
L-Phe
-
pH 8.0, 30C, wild-type enzyme
0.0245
-
L-Phe
-
isoenzyme PAL-3
0.027
-
L-Phe
-
-
0.027
-
L-Phe
-
pH 8.8, 30C, mutant enzyme Q487A
0.029
-
L-Phe
-
at low substrate substrate concentrations
0.03
-
L-Phe
-
tissue culture
0.032
-
L-Phe
-
at low concentrations
0.033
-
L-Phe
-
pH 8.8, 30C, mutant enzyme Y350F
0.038
-
L-Phe
-
at low substrate concentrations
0.04
-
L-Phe
-
enzyme form 1
0.043
-
L-Phe
-
at low substrate concentrations
0.043
-
L-Phe
-
-
0.044
-
L-Phe
-
at low substrate concentrations
0.052
-
L-Phe
-
at low substrate concentrations
0.055
-
L-Phe
-
two different Km-values: 0.011 mM and 0.055 mM
0.07
-
L-Phe
-
enzyme form 2
0.078
-
L-Phe
-
at high substrate concentrations
0.09
-
L-Phe
-
-
0.091
-
L-Phe
-
at high substrate concentrations
0.101
-
L-Phe
D3Y5L6
pH 8.5, 55C
0.11
-
L-Phe
-
enzyme form 3
0.12
-
L-Phe
-
pH 8.0, 30C, mutant enzyme V83A
0.121
-
L-Phe
-
enzyme form PAL-II
0.125
-
L-Phe
-, Q0GA81
pH 8.7, 37C
0.13
-
L-Phe
-
-
0.15
-
L-Phe
-
-
0.154
-
L-Phe
-
-
0.16
-
L-Phe
Streptomyces verticillatus
-
-
0.18
-
L-Phe
-
at low substrate concentrations
0.22
-
L-Phe
-
-
0.23
-
L-Phe
-, C0LL35, D5KS97
wild-type, pH 8.5, 37C
0.24
-
L-Phe
-
at high substrate concentrations
0.25
-
L-Phe
C0LL35
recombinant protein from Escherichia coli, pH 8.5, 37C
0.26
-
L-Phe
-
at high substrate concentrations
0.27
-
L-Phe
-
-
0.27
-
L-Phe
-
at high substrate concentrations
0.29
-
L-Phe
-
at high substrate concentrations
0.29
-
L-Phe
-
-
0.314
-
L-Phe
-
at 30C
0.331
-
L-Phe
C0LL35
recombinant protein from Pichia pastoris, pH 8.5, 37C
0.333
-
L-Phe
-, C0LL35, D5KS97
wild-type, pH 8.5, 37C
0.45
-
L-Phe
-
-
0.465
-
L-Phe
-
enzyme form PAL-III
0.5
-
L-Phe
Alternaria sp.
-
-
0.5
-
L-Phe
-
-
0.7
-
L-Phe
Alternaria sp.
-
-
0.8
-
L-Phe
-
at high substrate concentrationas
0.84
-
L-Phe
-
enzyme form PAL-I
1.05
-
L-Phe
-
-
1.7
-
L-Phe
-
-
2.07
-
L-Phe
-, C0LL35, D5KS97
pH 8.5, 37C
2.288
-
L-Phe
-, C0LL35, D5KS97
mutant F134H, pH 8.5, 37C
2.56
-
L-Phe
P45724, P45725, Q9SS45
pH 8.8, 31C
4.22
-
L-Phe
-, C0LL35, D5KS97
mutant F134H, pH 8.5, 37C
5
-
L-Phe
-
at high substrate concentrations
14.2
-
L-Phe
-
pH 8.8, 30C, mutant enzyme L137H
14.2
-
L-Phe
-
free enzyme, pH 8.7, 30C
15
-
L-Phe
Rhodotorula texensis
-
-
64.9
-
L-Phe
-
immobilized enzyme, pH 8.7, 30C
75.6
-
L-Phe
-
pH 8.8, 30C, mutant enzyme L137H/Q487E
0.028
-
L-phenylalanine
-
enzyme from fruit ripened at low temperature, first Km value using low substrate concentrations, pH 8.8, 30C
0.032
-
L-phenylalanine
-
pH 8.8, 30C
0.033
-
L-phenylalanine
-
-
0.0364
-
L-phenylalanine
C6ZIA5, P25872, P35513, P45733
isoform PAL3, at 30C in 50 mM Tris/HCl, pH 8.5
0.0395
-
L-phenylalanine
C6ZIA5, P25872, P35513, P45733
isoform PAL2, at 30C in 50 mM Tris/HCl, pH 8.5
0.04
-
L-phenylalanine
-
enzyme from fruit ripened at room temperature, pH 8.8, 30C
0.0428
-
L-phenylalanine
-
wild-type, pH 9.0, 37C
0.045
-
L-phenylalanine
-
wild-type, pH 8.5, 37C
0.049
-
L-phenylalanine
-
enzyme from fruit ripened in 20% CO2 atmosphere, first Km value using low substrate concentrations, pH 8.8, 30C
0.0524
-
L-phenylalanine
C6ZIA5, P25872, P35513, P45733
isoform PAL4, at 30C in 50 mM Tris/HCl, pH 8.5
0.0598
-
L-phenylalanine
C6ZIA5, P25872, P35513, P45733
isoform PAL1, at 30C in 50 mM Tris/HCl, pH 8.5
0.06
0.18
L-phenylalanine
-
enzyme from cultivar Verdial, in 37.5 mM borate buffer pH 8.8, at 40C
0.06
-
L-phenylalanine
-
mutant lacking 21 N-terminal amino acids, pH 8.5, 37C; wild-type, pH 8.5, 37C
0.06
-
L-phenylalanine
-
wild-type PAL
0.069
-
L-phenylalanine
-
mutant L108A, pH 8.5, 37C
0.07
-
L-phenylalanine
-
mutant L108G, pH 8.5, 37C
0.112
-
L-phenylalanine
-
enzyme from fruit ripened in 20% CO2 atmosphere, second Km value using high substrate concentrations, pH 8.8, 30C
0.112
-
L-phenylalanine
B5U983, -
pH 8.5, 37C, isozyme PAL3
0.12
0.25
L-phenylalanine
-
enzyme from cultivar Arbequina, in 37.5 mM borate buffer pH 8.8, at 40C
0.13
0.32
L-phenylalanine
-
enzyme from cultivar Frantonio, in 37.5 mM borate buffer pH 8.8, at 40C
0.144
-
L-phenylalanine
B5U983, -
pH 8.5, 37C, isozyme PAL2
0.152
-
L-phenylalanine
B5U983, -
pH 8.5, 37C, isozyme PAL1
0.164
-
L-phenylalanine
-
enzyme from fruit ripened at low temperature, second Km value using low substrate concentrations, pH 8.8, 30C
0.18
-
L-phenylalanine
B5U983, -
pH 8.5, 37C, isozyme PAL4
0.23
0.3
L-phenylalanine
-
enzyme from cultivar Picual, in 37.5 mM borate buffer pH 8.8, at 40C
0.25
-
L-phenylalanine
Q2VMT1
-
0.25
-
L-phenylalanine
C0LL35
recombinant enzyme expressed in Escherichia coli; recombinant enzyme expressed in Escherichia coli, at 37C and pH 8.5
0.331
-
L-phenylalanine
C0LL35
recombinant enzyme expressed in Pichia pastoris, at 37C and pH 8.5; recombinant enzyme expressed in Pichi pastoris
0.5
-
L-phenylalanine
-
mutant F137V, pH 10, 30C
0.6
-
L-phenylalanine
-
wild-type, pH 10, 30C
1.01
-
L-phenylalanine
-
recombinant enzyme, in 50 mM Tris-HCl, pH 8.5, at 37C
1.33
1.75
L-phenylalanine
-
in presence or absence of D-phenylalanine
1.386
-
L-phenylalanine
-
mutant F144H, pH 9.0, 37C
0.097
-
L-Tyr
-, C0LL35, D5KS97
pH 8.5, 37C
0.335
-
L-Tyr
-, C0LL35, D5KS97
mutant F134H, pH 8.5, 37C
0.993
-
L-Tyr
-, C0LL35, D5KS97
wild-type, pH 8.5, 37C
1.31
-
L-Tyr
-, Q0GA81
pH 8.7, 37C
2.3
-
L-Tyr
-
isoenzyme PAL-2
2.5
-
L-Tyr
-
isoenzyme PAL-1
2.6
-
L-Tyr
-
isoenzyme PAL-4
7.8
-
L-Tyr
-
isoenzyme PAL-3
0.4
-
L-tyrosine
-
wild-type, pH 10, 30C
0.532
-
L-tyrosine
-
mutant F144H, pH 9.0, 37C
1.049
-
L-tyrosine
-
wild-type, pH 9.0, 37C
0.022
-
L-[3-H1]-Phe
-
pH 8.8, 30C, mutant enzyme Q487A
0.028
-
L-[3-H1]-Phe
-
pH 8.8, 30C, mutant enzyme Y350F
9.8
-
L-[3-H1]-Phe
-
pH 8.8, 30C, mutant enzyme L137H
6.6
-
N-methyl-L-phenylalanine
-
-
2.6
-
NH3
-
pH 10.0
4.4
-
NH3
-
pH 8.8
0.05
-
phenylalanine
-
C503S/C565S mutant PAL
42.4
-
L-[3-H1]-Phe
-
pH 8.8, 30C, mutant enzyme L137H/Q487E
additional information
-
additional information
-
influence of assay conditions on the Km-value
-
additional information
-
additional information
-
Michaelis-Menten kinetics
-
additional information
-
additional information
Q2VMT1
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
L-Phe
P45724, P45725, Q9SS45
pH 8.8, 31C
1.73
-
L-Phe
-, Q0GA81
pH 8.7, 37C
1.8
-
L-Phe
P45724, P45725, Q9SS45
pH 8.4, 37C
3
-
L-Phe
P45724, P45725, Q9SS45
pH 8.4, 37C
3.2
-
L-Phe
P45724, P45725, Q9SS45
pH 8.4, 37C
3.36
-
L-Phe
D3Y5L6
pH 8.5, 55C
4.79
-
L-Phe
-
pH 8.0, 30C, wild-type enzyme
7.8
-
L-Phe
-, C0LL35, D5KS97
mutant F134H, pH 8.5, 37C
10.12
-
L-Phe
C0LL35
recombinant protein from Escherichia coli, pH 8.5, 37C
16.04
-
L-Phe
C0LL35
recombinant protein from Pichia pastoris, pH 8.5, 37C
16.3
-
L-Phe
-, C0LL35, D5KS97
wild-type, pH 8.5, 37C
16.32
-
L-Phe
-, C0LL35, D5KS97
pH 8.5, 37C
19.2
-
L-Phe
-, C0LL35, D5KS97
mutant F134H, pH 8.5, 37C
21.3
-
L-Phe
-, C0LL35, D5KS97
wild-type, pH 8.5, 37C
0.362
-
L-phenylalanine
B5U983, -
pH 8.5, 37C, isozyme PAL3
0.457
-
L-phenylalanine
B5U983, -
pH 8.5, 37C, isozyme PAL2
0.516
-
L-phenylalanine
B5U983, -
pH 8.5, 37C, isozyme PAL4
0.588
-
L-phenylalanine
B5U983, -
pH 8.5, 37C, isozyme PAL1
0.78
-
L-phenylalanine
C6ZIA5, P25872, P35513, P45733
isoform PAL3, at 30C in 50 mM Tris/HCl, pH 8.5
0.95
-
L-phenylalanine
-
mutant L108G, pH 8.5, 37C
1.09
-
L-phenylalanine
C6ZIA5, P25872, P35513, P45733
isoform PAL1, at 30C in 50 mM Tris/HCl, pH 8.5
1.14
-
L-phenylalanine
C6ZIA5, P25872, P35513, P45733
isoform PAL2, at 30C in 50 mM Tris/HCl, pH 8.5
1.53
-
L-phenylalanine
C6ZIA5, P25872, P35513, P45733
isoform PAL4, at 30C in 50 mM Tris/HCl, pH 8.5
1.96
-
L-phenylalanine
-
wild-type, pH 8.5, 37C
3.6
-
L-phenylalanine
-
mutant L108A, pH 8.5, 37C
4.4
-
L-phenylalanine
-
wild-type, pH 8.5, 37C
4.6
-
L-phenylalanine
-
mutant lacking 21 N-terminal amino acids, pH 8.5, 37C
4.6
-
L-phenylalanine
-
wild-type PAL
10.11
-
L-phenylalanine
-
recombinant enzyme, in 50 mM Tris-HCl, pH 8.5, at 37C
10.12
-
L-phenylalanine
C0LL35
recombinant enzyme expressed in Escherichia coli; recombinant enzyme expressed in Escherichia coli, at 37C and pH 8.5
16.04
-
L-phenylalanine
C0LL35
recombinant enzyme expressed in Pichia pastoris, at 37C and pH 8.5; recombinant enzyme expressed in Pichi pastoris
47.3
-
L-phenylalanine
-
mutant F144H, pH 9.0, 37C
65
-
L-phenylalanine
-
wild-type, pH 9.0, 37C
115.8
-
L-phenylalanine
-
wild-type, pH 9.0, 37C
0.03
-
L-Tyr
-, C0LL35, D5KS97
wild-type, pH 8.5, 37C
0.1
-
L-Tyr
-, C0LL35, D5KS97
mutant F134H, pH 8.5, 37C
0.11
-
L-Tyr
-, Q0GA81
pH 8.7, 37C
0.3
-
L-Tyr
-
30C
0.54
-
L-Tyr
-, C0LL35, D5KS97
pH 8.5, 37C
0.084
-
L-tyrosine
-
wild-type, pH 9.0, 37C
0.75
-
L-tyrosine
-
mutant F144H, pH 9.0, 37C
0.22
-
N-methyl-L-phenylalanine
-
-
4
-
phenylalanine
-
C503S/C565S mutant PAL
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.18
-
L-Phe
-, C0LL35, D5KS97
mutant F134H, pH 8.5, 37C
12354
7.88
-
L-Phe
-, C0LL35, D5KS97
pH 8.5, 37C
12354
8.4
-
L-Phe
-, C0LL35, D5KS97
mutant F134H, pH 8.5, 37C
12354
13.8
-
L-Phe
-, Q0GA81
pH 8.7, 37C
12354
33.17
-
L-Phe
D3Y5L6
pH 8.5, 55C
12354
40.5
-
L-Phe
C0LL35
recombinant protein from Escherichia coli, pH 8.5, 37C
12354
48.5
-
L-Phe
C0LL35
recombinant protein from Pichia pastoris, pH 8.5, 37C
12354
63.9
-
L-Phe
-, C0LL35, D5KS97
wild-type, pH 8.5, 37C
12354
70.8
-
L-Phe
-, C0LL35, D5KS97
wild-type, pH 8.5, 37C
12354
4.05
-
L-phenylalanine
C0LL35
recombinant enzyme expressed in Escherichia coli
12364
4.85
-
L-phenylalanine
C0LL35
recombinant enzyme expressed in Pichi pastoris
12364
10
-
L-phenylalanine
-
recombinant enzyme, in 50 mM Tris-HCl, pH 8.5, at 37C
12364
18.28
-
L-phenylalanine
C6ZIA5, P25872, P35513, P45733
isoform PAL1, at 30C in 50 mM Tris/HCl, pH 8.5
12364
21.1
-
L-phenylalanine
C6ZIA5, P25872, P35513, P45733
isoform PAL3, at 30C in 50 mM Tris/HCl, pH 8.5
12364
28.93
-
L-phenylalanine
C6ZIA5, P25872, P35513, P45733
isoform PAL2, at 30C in 50 mM Tris/HCl, pH 8.5
12364
29.09
-
L-phenylalanine
C6ZIA5, P25872, P35513, P45733
isoform PAL4, at 30C in 50 mM Tris/HCl, pH 8.5
12364
0.028
-
L-Tyr
-, C0LL35, D5KS97
wild-type, pH 8.5, 37C
12441
0.08
-
L-Tyr
-, Q0GA81
pH 8.7, 37C
12441
0.31
-
L-Tyr
-, C0LL35, D5KS97
mutant F134H, pH 8.5, 37C
12441
5.56
-
L-Tyr
-, C0LL35, D5KS97
pH 8.5, 37C
12441
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00008
-
(+)-1-amino-3',4'-dichlorobenzylphosphonic acid
-
-
0.0089
-
(+-)-2-aminomethyl-3-phenylpropanoic acid
-
40C, pH 8.8
0.013
-
(2S)-2-amino-3-(1-benzofuran-3-yl)propanoic acid
-
pH 8.8, 30C
0.007
-
(2S)-2-amino-3-(1-benzothien-3-yl)propanoic acid
-
pH 8.8, 30C
0.001
-
(R)-1-amino-2-(4-fluorophenyl)ethylphosphonic acid
-
40C, pH 8.8
0.00000038
-
(S)-2-aminooxy-3-phenylpropanoic acid
-
40C, pH 8.8
0.025
-
2-amino-3-(1-benzofuran-3-yl)propanoic acid
-
pH 8.8, 30C
0.016
-
2-amino-3-(1-benzothien-3-yl)propanoic acid
-
pH 8.8, 30C
0.00009
-
2-amino-4-bromoindane-2-phosphonic acid
-
-
0.00195
-
2-amino-4-hydroxyindane-2-phosphonic acid
-
-
0.0019
-
2-aminoindan-2-carboxylic acid
-
40C, pH 8.8
0.000025
-
2-aminoindan-2-phosphonic acid
-
40C, pH 8.8
0.000056
-
2-aminoindan-2-phosphonic acid
D3Y5L6
pH 8.5, 55C
0.00191
-
2-aminoindan-2-phosphonic acid
-
-
0.00008
-
2-aminoindane-2-phosphonic acid
-
-
0.00012
-
2-aminoindane-2-phosphonic acid
-
30C, pH 8.8
3
-
2-mercaptoethanol
C6ZIA5, P25872, P35513, P45733
isoform PAL1; isoform PAL1
7
-
beta-(2-pyrimidinyl)-D,L-alanine
-
-
0.043
-
chlorogenic acid
D3Y5L6
pH 8.5, 55C
0.008
-
Cinnamic acid
D3Y5L6
pH 8.5, 55C
0.037
-
cinnamyl alcohol
D3Y5L6
pH 8.5, 55C
0.032
-
coniferyl alcohol
D3Y5L6
pH 8.5, 55C
0.013
-
coniferyl aldehyde
D3Y5L6
pH 8.5, 55C
0.032
-
coumaric acid
D3Y5L6
pH 8.5, 55C
3.3
-
D-phenylalanine
Q2VMT1
-
0.000008
-
N,N-dimethyl-4-nitro-L-phenylalanine
-
-
0.00013
-
N-methyl-4-nitro-L-phenylalanine
-
-
0.017
-
salidroside
D3Y5L6
pH 8.5, 55C
3.38
-
D-phenylalanine
-
-
additional information
-
additional information
-
inhibition kinetics
-
additional information
-
additional information
Q2VMT1
inhibition kinetics
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0339
-
2-amino-4-bromoindane-2-phosphonic acid
-
-
0.06
-
2-amino-4-hydroxyindane-2-phosphonic acid
-
-
0.0015
-
2-aminoindane-2-phosphonic acid
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0000115
-
B5U983, -
aerial plant parts
0.0000783
-
B5U983, -
roots
0.0256
-
Q8VXG7, -
average PAL-specific activity of roots from 46-days-old plants
0.14
-
-
immobilized enzyme, pH 8.7, 30C
0.19
-
C0LL35
crude recombinant extract from Escherichia coli, at 37C and pH 8.5
0.39
-
-
free enzyme, pH 8.7, 30C
0.41
-
C0LL35
crude recombinant extract from Pichia pastoris, at 37C and pH 8.5
0.425
-
-
-
1.07
2.5
Q2VMT1
-
1.7
-
-
wild-type PAL
2.2
-
-
C503S/C565S mutant PAL
3.76
-
C0LL35
recombinant enzyme from Pichia pastoris, after 9.1fold purification, at 37C and pH 8.5; recombinant protein from Pichia pastoris, pH 8.5, 37C
3.77
-
C0LL35
recombinant enzyme expressed in Escherichia coli; recombinant protein from Escherichia coli, pH 8.5, 37C
3.78
-
C0LL35
recombinant enzyme from Escherichia coli, after 19.4fold purification, at 37C and pH 8.5
26.6
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
specific activity increases approx. 3fold in seedlings after investating with the aphid Shizaphis grinum
additional information
-
-
PAL activity is induced 3-5fold upon growth on L-tryptophan
additional information
-
-
relative enzyme activity after different storage conditions, overview
additional information
-
-
-
additional information
-
-
relative enzyme activity and encapsulation efficiency in microcapsules, overview
additional information
-
Q43210
tissue specific enzyme activity per g fresh weight, overview
additional information
-
-
activity in seeds during maturation, overview
additional information
-
-
44.5 U/mg protein, 1 unit is defined as the amount of enzyme causing an increase in absorbtion
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
8.5
-
C503S/C565S mutant PAL
7.7
-
-
-
7.8
-
-
assay at
8
-
-, C0LL35, D5KS97
;
8.2
-
Alternaria sp.
-
enzyme form PAL68
8.4
8.8
P45724, P45725, Q9SS45
-
8.4
8.9
P45724, P45725, Q9SS45
-
8.4
9.2
P45724, P45725, Q9SS45
-
8.5
9
C0LL35
-
8.5
9.5
-
-
8.5
-
Streptomyces verticillatus
-
-
8.5
-
B5U983, -
assay at
8.5
-
-
assay at
8.5
-
C0LL35
recombinant enzyme expressed in Escherichia coli
8.5
-
D3Y5L6
-
8.6
-
-
-
8.7
8.9
P45724, P45725, Q9SS45
-
8.7
-
-, Q0GA81
-
8.8
9.2
-
-
8.8
-
-
tissue culture
8.8
-
Alternaria sp.
-
enzyme form PAL116
8.8
-
-
enzyme form PAL-II
8.8
-
-
forward reaction
8.8
-
-
assay at
8.8
-
-
assay at
8.8
-
-, Q52QH3
assay at
8.8
-
Q43210
assay at
8.8
-
P11544
assay at
8.8
-
P35511
assay at
8.8
-
-
assay at
8.8
-
-
assay at
8.9
-
-
-
8.9
-
-
assay at
8.9
-
Q2VMT1
assay at
8.9
-
-
assay at
8.9
-
P45735
assay at
9
-
Rhodotorula glutinis, Rhodotorula texensis
-
-
9
-
-
reverse reaction
9
-
C0LL35
recombinant enzyme expressed in Pichi pastoris
9
-
-, C0LL35, D5KS97
-
9.5
-
-
enzyme form PAL-III
10
-
-
assay at
10.5
-
-
enzyme form PAL-I
10.6
-
Rhodococcus rubra, Rhodotorula mucilaginosa
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
12
-
pH-dependent activity profile
6.8
9.2
-
pH 6.5: 50% of maximal activity, pH 8.8-9.2: optimum
7
10
-
pH 7: about 40% of maximal activity, pH 10: about 85% of maximal activity
7
10
-
pH 7: about 30% of maximal activity, pH 10: about 65% of maximal activity
7
10
-
forward and reverse reactions
7
10.5
-
pH 7: about 35% of maximal activity, pH 10.5: about 70% of maximal activity
7
10.5
-
pH 7: about 30% of maximal activity, pH 10.5: about 90% of maximal activity, enzyme form PAL-III; pH 7: about 50% of maximal activity, pH 10.5: about 70% of maximal activity, enzyme form PAL-II
7
11
-
pH 7: about 50% of maximal activity, pH 11: about 70% of maximal activity
7.5
10.5
-
-
7.5
9
-
pH 7.5: about 70% of maximal activity, pH 9.0: about 70% of maximal activity
8
11
-
pH 8: about 50% of maximal activity, pH 11: about 80% of maximal activity, enzyme form PAL-I
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
Rhodococcus rubra, Rhodotorula mucilaginosa
-
-
30
-
-
forward and reverse reactions
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
Q2VMT1
assay at
30
-
P11544
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
31
-
P45724, P45725, Q9SS45
-
36
48
P45724, P45725, Q9SS45
-
37
-
B5U983, -
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
Q43210
assay at
37
-
-
assay at
37
-
P45735
assay at
37
-
P35511
assay at
40
-
-, Q52QH3
assay at
40
-
-
assay at
46
48
P45724, P45725, Q9SS45
-
48
-
P45724, P45725, Q9SS45
-
50
60
C0LL35
-
50
-
-
-
50
-
C0LL35
recombinant enzyme expressed in Escherichia coli
50
-
-, C0LL35, D5KS97
-
60
-
C0LL35
recombinant enzyme expressed in Pichi pastoris
60
-
-, Q0GA81
-
60
-
-, C0LL35, D5KS97
;
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
60
-
15C: about 25% of maximal activity, 60C: no activity
30
60
-
30C: about 45% of maximal activity, 60C: about 30% of maximal activity
additional information
-
-, Q52QH3
accumulation of mRNA for calycosin-7-O-beta-Dglucoside pathway genes during different temperature treatments, overview
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
P35511
isozyme PAL-II, isoelectric focusing
5.5
-
P35511
isozyme PAL-III, isoelectric focusing
5.9
-
-, C0LL35, D5KS97
calculated; calculated
5.96
-
A7UHB6
sequence calculation
6.1
-
F8RL28
calculated
6.2
-
-, Q0GA81
calculated
6.31
-
A9XIW5
sequence calculation
6.5
-
Q5EIB6, -
sequence calcualtion
6.8
-
C6ZIA5, P25872, P35513, P45733
isoform PAL1 with His-tag, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
in Penicillium digitatum non-infected areas, the actvities of superoxide dismutase, EC 1.15.1.1, catalase, EC 1.11.1.6, ascorbate peroxidase, EC 1.11.1.11, and glutathione reductase, EC 1.6.4.2, as well as soluble and insoluble peroxidase, EC 1.11.1.7, and phenylalanine ammonia-lyase, EC 4.3.1.24 are higher in flavedo than in alvedo
Manually annotated by BRENDA team
Tulipa hybrid cultivar Appeldoorn
-
-
-
Manually annotated by BRENDA team
B9VR52
high expression, expression levels increase in the order green leaves, turning color leaves, bracts. Diurnal variation of PAL expression level in bracts exhibits two highest peaks at 9:00 and 18:00, respectively, and reaches the lowest level at 12:00 in a clear day
Manually annotated by BRENDA team
Euphorbia pulcherrima willd.
-
high expression, expression levels increase in the order green leaves, turning color leaves, bracts. Diurnal variation of PAL expression level in bracts exhibits two highest peaks at 9:00 and 18:00, respectively, and reaches the lowest level at 12:00 in a clear day
-
Manually annotated by BRENDA team
-, E3T9X0
low expression
Manually annotated by BRENDA team
A0MQ91, -
level of enzyme mRNA increases 5 days after the establishment of in vitro callus unions. Enzyme transcription shows a higher level in graft union of incompatible partners and does not result in formation of lignin
Manually annotated by BRENDA team
A0MQ92
level of enzyme mRNA increases 5 days after the establishment of in vitro callus unions. Enzyme transcription shows a higher level in graft union of incompatible partners and does not result in formation of lignin
Manually annotated by BRENDA team
-
VB2 and VB1 callus cultures
Manually annotated by BRENDA team
-
kinetin-treated and untreated cells
Manually annotated by BRENDA team
B0M0P5, Q852S1
; DcPAL3 gene expression occurs in anthocyanin-synthesizing cells
Manually annotated by BRENDA team
Q43210
from seddlings, 74 kDa isozyme
Manually annotated by BRENDA team
-
in Penicillium digitatum non-infected areas, the actvities of superoxide dismutase, EC 1.15.1.1, catalase, EC 1.11.1.6, ascorbate peroxidase, EC 1.11.1.11, and glutathione reductase, EC 1.6.4.2, as well as soluble and insoluble peroxidase, EC 1.11.1.7, and phenylalanine ammonia-lyase, EC 4.3.1.24 are higher in flavedo than in alvedo. Upon infection, phenylalanine ammonia-lyase activity and transcript level in flavedo increases, but Penicillium digitatum can suppress this defencse response
Manually annotated by BRENDA team
-
transcripts of RiPAL1 and RiPAL2
Manually annotated by BRENDA team
B9VU66
transcript levels are higher in bud flowers and wilting flowers than in blooming flowers
Manually annotated by BRENDA team
-, Q0GA81
highest expression
Manually annotated by BRENDA team
-
transcripts of RiPAL1 and RiPAL2
Manually annotated by BRENDA team
P45735
berry
Manually annotated by BRENDA team
F8RL28
expression of isoform PAL6 is fruit-specific, and increases during fruit ripening in both cultivars along with anthocyanin accumulation. PAL enzyme activity increases at similar rates in both cultivars at early ripening stages, but at the end of ripening PAL activity diminishes in cultivar Toyonoka while it rises markedly in cultivar Camarosa. PAL activity is higher in internal fruit tissue, showing no correlation with anthocyanin level of the same section in both cultivars. The higher FaPAL6 expression and activity detected in Camarosa may be associated to the enhanced anthocyanin accumulation found in this cultivar
Manually annotated by BRENDA team
-
induced by a Verticillium dahliae phytotoxin
Manually annotated by BRENDA team
-
sheath tissue of shoots
Manually annotated by BRENDA team
-
very low levels of RiPAL transcripts
Manually annotated by BRENDA team
-
transcripts for the wound-inducible enzyme LsPAL1 accumulate in cells close to the wound sites. PAL mRNA is associated with tissue next to the epidermis and vascular bundles
Manually annotated by BRENDA team
Q672H7
PAL expression is constitutive in leaves throughout development and decline only in the most mature stage, overview
Manually annotated by BRENDA team
A7UHB6
high expression level
Manually annotated by BRENDA team
Q43210
from seedlings, three isozymes of 74 kDa, 83 kDa, and 103 kDa molecular weight
Manually annotated by BRENDA team
C6ZIA5, P25872, P35513, P45733
-
Manually annotated by BRENDA team
B9VR52
low expression, expression levels increase in the order green leaves, turning color leaves, bracts
Manually annotated by BRENDA team
-, Q0GA81
expression in all tissues tested, most highly in flowers, followed by stem and leaf, and lowest in root and seed
Manually annotated by BRENDA team
Alternaria sp.
-
2 different enzyme forms are isolated after 68 h and after 116 h: PAL68 and PAL116
Manually annotated by BRENDA team
C6ZIA5, P25872, P35513, P45733
-
Manually annotated by BRENDA team
C6ZIA5, P25872, P35513, P45733
-
Manually annotated by BRENDA team
-
transcripts of RiPAL1 and RiPAL2
Manually annotated by BRENDA team
-
uncut and shredded carrots. Enzyme activity is induced by processing and linearly increased throughout storage under aerobic conditions. An anaerobic atmosphere results in a maximum activity peak at storage day 2-4. The use of chlorinated water for washing shredded carrots slightly delays the onset of PAL activity
Manually annotated by BRENDA team
Q43210
from seedlings, 74 kDa isozyme
Manually annotated by BRENDA team
Q5EIB6, -
low expression level
Manually annotated by BRENDA team
C6ZIA5, P25872, P35513, P45733
-
Manually annotated by BRENDA team
Q8VXG7, -
the root tissues of the corn variety Japanese Striped corn contain greater levels of PAL gene transcripts and PAL activities, compared to those of the shoot tissues
Manually annotated by BRENDA team
-, E3T9X0
higest expression
Manually annotated by BRENDA team
-, F4YRL1
highly expressed in fine roots
Manually annotated by BRENDA team
B9VR52
high expression
Manually annotated by BRENDA team
-, Q0GA81
expression in all tissues tested, most highly in flowers, followed by stem and leaf, and lowest in root and seed
Manually annotated by BRENDA team
-
cultured Morinda citrifolia adventitious roots in different strength, i.e. 0.25, 0.50, 0.75, 1.0, 1.5 and 2.0 of Murashige and Skoog medium supplemented with 5 mg/l indole butyric acid and 30 g/l sucrose
Manually annotated by BRENDA team
Euphorbia pulcherrima willd.
-
high expression
-
Manually annotated by BRENDA team
-
enzyme activity changes during seed maturation and decreases steadily for up to 15 weeks after flowering from 336 to 211 U per g fresh weight, inverse relationship between enzyme protein content and activity
Manually annotated by BRENDA team
-, Q0GA81
expression in all tissues tested, most highly in flowers, followed by stem and leaf, and lowest in root and seed
Manually annotated by BRENDA team
-
PAL activity is greatly induced by mechanical wounding and aphid infestation in cotton seedlings. The iduction of PAL occurs not only in wounded and infested seedlings but also in intact healthy seddlings growing nearby
Manually annotated by BRENDA team
-
with four expanded leaves
Manually annotated by BRENDA team
Q43210
7-days-old
Manually annotated by BRENDA team
Q8VXG7, -
the PAL activity of young seedlings of the corn variety Indian Blue corn is generally 30-50% lower than those of cultivar Japanese Striped corn seedlings at equivalent growth stages
Manually annotated by BRENDA team
Gossypium hirsutum Zhongmian 35
-
PAL activity is greatly induced by mechanical wounding and aphid infestation in cotton seedlings. The iduction of PAL occurs not only in wounded and infested seedlings but also in intact healthy seddlings growing nearby
-
Manually annotated by BRENDA team
-, C0LL35, D5KS97
-
Manually annotated by BRENDA team
-
transcripts of RiPAL1 and RiPAL2
Manually annotated by BRENDA team
Q8VXG7, -
the shoot tissues of the corn variety Japanese Striped corn contain lower levels of PAL gene transcripts and PAL activities, compared to those of the root tissues
Manually annotated by BRENDA team
-, C0LL35, D5KS97
in shoot and branch shoot, mainly localized to sclerenchymal cells; in shoot and branch shoot, mainly loclaized to sclerenchymal cells; in shoot and branch shoot, mainly loclaized to sclerenchymal cells
Manually annotated by BRENDA team
C6ZIA5, P25872, P35513, P45733
-
Manually annotated by BRENDA team
A7UHB6
high expression level
Manually annotated by BRENDA team
B9VR52
low expression
Manually annotated by BRENDA team
-, Q0GA81
expression in all tissues tested, most highly in flowers, followed by stem and leaf, and lowest in root and seed
Manually annotated by BRENDA team
Euphorbia pulcherrima willd.
-
low expression
-
Manually annotated by BRENDA team
C6ZIA5, P25872, P35513, P45733
-
Manually annotated by BRENDA team
-
diffenrentiating secondary xylem
Manually annotated by BRENDA team
C6ZIA5, P25872, P35513, P45733
-
Manually annotated by BRENDA team
Euphorbia pulcherrima willd.
-
low expression, expression levels increase in the order green leaves, turning color leaves, bracts
-
Manually annotated by BRENDA team
additional information
A7UHB6
broad and constitutive tissue expression, temporal expression profiling analysis, overview
Manually annotated by BRENDA team
additional information
B5U983, -
the expression of pal genes in the roots is higher than in the plants aerial parts, the activity of PAL in the roots is also higher than in the aerial parts
Manually annotated by BRENDA team
additional information
Q8VXG7, -
dry seeds of both varieties have no PAL activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoenzyme PAL1 and PAL2. Overexpression of cinnamate 4-hydroxylase results in reorganization of PAL2 localization from cytosol to endoplasmic reticulum
Manually annotated by BRENDA team
-
both in plastid and cytosol of xylem ray parenchymal cells and in cytosol of the developing xylem cells of the mature stem
Manually annotated by BRENDA team
-
colocalization of L-phenylalanine ammonia-lyase and cinnamate 4-hydroxylase on ER membranes. Overexpression of cinnamate 4-hydroxylase results in reorganization of PAL2 localization from cytosol to endoplasmic reticulum
Manually annotated by BRENDA team
Quercus pedunculata
-
-
Manually annotated by BRENDA team
-
; isoenzyme PAL1
-
Manually annotated by BRENDA team
Quercus pedunculata, Ricinus communis
-
-
Manually annotated by BRENDA team
-
both in plastid and cytosol of xylem ray parenchymal cells
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70000
-
C6ZIA5, P25872, P35513, P45733
SDS-PAGE; SDS-PAGE; SDS-PAGE; SDS-PAGE
74000
-
Q43210
-
76950
-
-
subunit, calculated from amino acid sequence
76970
-
C0LL35
subunit, calculated from amino acid sequence
83000
-
Q43210
-
103000
-
Q43210
-
170000
-
-
gel filtration
225000
-
-
non-denaturing gradient PAGE
226000
-
Streptomyces verticillatus
-
-
255000
-
-
gel filtration
262000
-
C6ZIA5, P25872, P35513, P45733
PAL1 with a C-terminal His-tag, gel filtration
266000
-
-
gel filtration
275000
330000
-
-
280000
-
-
-
280000
-
-
gel filtration
290000
-
-, C0LL35, D5KS97
gel filtration
300000
-
-
isoenzyme PAL 1, gel filtration
306000
-
-
-
311000
-
-
gel filtration
316000
-
-
-
316000
-
-
non-denaturing gradient PAGE
320000
-
-
-
320000
-
-
gel filtration
320000
-
-
gel filtration
320000
-
-
gel filtration
320000
-
-
non-denaturing PAGE
320000
-
-
gel filtration
320000
-
-, C0LL35, D5KS97
gel filtration
323000
-
-
gel filtration
324000
-
-
gel filtration
330000
-
-
-
330000
-
-
-
330000
-
-
gel filtration
330000
-
C0LL35
gel filtration; PAGE and gel filtration; SDS-PAGE
330000
-
-, C0LL35, D5KS97
gel filtration
332000
-
-
gel filtration
336000
-
-
non-denaturing PAGE with 5-10% acrylamide
337500
-
-
non-denaturing PAGE with 4-20% acrylamide
340000
-
-
density gradient centrifugation
354000
-
-
non-denaturing PAGE
360000
-
-
non-denaturing PAGE
380000
-
Alternaria sp.
-
enzyme form PAL116, gel filtration
560000
-
Alternaria sp.
-
enzyme form PAL68, gel filtration
additional information
-
Q43210
wheat seedlings contain isozymes of 74 kDa, 83 kDa, and 103 kDa molecular weight
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 77000, multiple MW-forms: 83000 Da and 77000 Da, SDS-PAGE; x * 83000, multiple MW-forms: 83000 Da and 77000 Da, SDS-PAGE
?
-
x * 80000, SDS-PAGE
?
-
x * 83000, SDS-PAGE
?
-
x * 70000 + x * 90000, SDS-PAGE
?
-
x * 83000, SDS-PAGE
?
-
x * 75000 + x * 80000, SDS-PAGE
?
-
x * 83000, SDS-PAGE
?
-
x * 75000, SDS-PAGE
?
-
x * 86000, SDS-PAGE
?
-
x * 72000, SDS-PAGE
?
-
x * 78000, SDS-PAGE
?
-
x * 60000, SDS-PAGE
?
P45724, P45725, Q9SS45
x * 76900, SDS-PAGE; x * 77600, SDS-PAGE; x * 78700, SDS-PAGE; x * 79100, His6-tagged enzyme, SDS-PAGE
?
A7UHB6
x * 79100, sequence calculation
?
B5U983, -
x * 79000, about, PAL isozymes, sequence calculation
?
A9XIW5
x * 77105, sequence calculation
?
-
x * 70000, SDS-PAGE
?
Q5EIB6, -
x * 77450, PALrs1, sequence calcualtion
?
P35511
x * 80000, SDS-PAGE
?
-, E3T9X0
x * 77000, calculated
?
-, F4YRL1
x * 67020, calculated
?
D3Y5L6
x * 94000, SDS-PAGE of recombinant protein with GST-tag
?
-, Q0GA81
x * 77300, calculated
?
F8RL28
x * 78139, calculated
heterotetramer
C6ZIA5, P25872, P35513, P45733
-
homotetramer
-
4 * 80000, subunit, SDS-PAGE
tetramer
-
4 * 70000
tetramer
-
4 * 86000, SDS-PAGE
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
alpha2,beta2, 2 * 70000 + 2 * 90000, SDS-PAGE
tetramer
-
alpha2,beta2, 2 * 75000 + 2 * 85000, SDS-PAGE
tetramer
-
4 * 83000, SDS-PAGE
tetramer
-
4 * 80000, SDS-PAGE
tetramer
-
4 * 77000, SDS-PAGE
tetramer
-
4 * 74000, SDS-PAGE
tetramer
-
4 * 80000, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
4 * 38000, SDS-PAGE
tetramer
-
4 * 77828, calculation from nucleotide sequence
tetramer
-
4 * 64000, SDS-PAGE, recombinant enzyme with His-tag, and crystallization data
tetramer
-
4 * 80000, SDS-PAGE
tetramer
Q43210
wheat seedlings contain isozymes of 74 kDa, 83 kDa, and 103 kDa molecular weight
tetramer
C0LL35
4 * 76970, calculated, 4 * 80000, SDS-PAGE of recombinant protein with His-tag; 4 * 80000, SDS-PAGE
tetramer
-, C0LL35, D5KS97
4 * 75711, calculated; 4 * 76950, calculated, 4 * 76000, SDS-PAGE; 4 * 76975, calculated, 4 * 76000, SDS-PAGE
homotetramer
C0LL35
4 * 80000, SDS-PAGE
additional information
A9XIW5
tertiary structure of SmPAL1, homology-based modeling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
Q43210
PAL exhibits three potential sites for N-linked glycosylation
no modification
-
no glycosylation
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
C503S/C565S mutant PAL, sitting drop vapor diffusion method, 25C, mixing of equal volumes of 300 nl of protein and reservoir solutions, the latter containing 12-20% PEG 1500 and 100 mM succinic acid, sodium dihydrogen phosphate, and glycine, pH 7.0, versus 0.07 ml of reservoir solution, cryoprotection by 25% glucose, X-ray diffraction structure determination and analysis at 1.87 A resolution, modeling
-
space group P1, 1.9 A resolution. Enzyme exists as homotetramer. Comparison with enzyme from Nostoc punctiforme
-
space group I222, 2.5 A resolution. Enzyme exists as homotetramer. Comparison with enzyme from Anabaena variabilis
-
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
P24481
molecular dynamics studies. The Tyr61-loop-in model is conformationally stable and assumed to be the active form. Deletion of the C-terminal multi-helix domain results in a significantly more rigid Tyr-loop-in structure. Comparison with strucutural models of Petroselinum crispum and Streptomyces maritimus enzymes
-
hanging-drop vapor diffusion method
-
molecular dynamics studies. The Tyr61-loop-in model is conformationally stable and assumed to be the active form. Deletion of the C-terminal multi-helix domain results in a significantly more rigid Tyr-loop-in structure. Comparison with strucutural models of Petroselinum crispum and Photorhabdus luminescens enzymes
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.5
9.5
-
1 h, loss of about 50% activity at pH 2.5, and of 38% at pH 9.5, highly stable at pH 8.8, in absence of L-Phe, but loss of about 50% activity after 30 min in presence of L-Phe
6.55
-
-
most stable at
6.55
-
Q2VMT1
most stable at
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
40% and 90% loss of activity after 1 and 5 days, respectively; approx. 30% loss of activity after 5 days in the presence of 30% glycerol
50
-
-
pH 7.0, 10 min, stable
57
-
-
15 min, loss of 50% activity
57
-
Q2VMT1
15 min, loss of 50% activity
60
-
-
20% glycerol increases half-life from 0.78 h to 1.4 h
60
-
-
pH 7.0, 10 min, 30% loss of activity
65
-
-
10 min, loss of activity
70
-
-
pH 7.0, 10 min, complete loss of activity
70
-
D3Y5L6
20 min, retains more than 85% of activity
75
-
D3Y5L6
20 min, loss of more than 85% of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme stabilization by 20% glycerol, 2-mercaptoethanol at 10 mM, 5 mM EDTA, and 2% ascorbic acid or 5 mM EDTA + 2% ascorbic acid
-
glycerol stabilizes the enzyme
Q2VMT1
the plant cell walls provide protection of PAL during in vitro digestion
-
roots retain 90% of their PAL activity after freeze-drying and about 40-60% activity after freeze-drying and a subsequent 15-week storage at 4C
Q8VXG7, -
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Glycerol
-
stabilizes
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Due to the instability of the enzyme towards oxygen, the biotransformation is performed under anaerobic, static conditions
Rhodococcus rubra, Rhodotorula mucilaginosa
-
660529
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
6C, almost complete loss of cooperativity after 7 days
-
0-5C, stable
-
-10C, 25% loss of activity after 3.5 months
-
2-aminoindan-2-phosphonic acid strongly inhibits PAL activity, such that PAL activity is reduced to about 48.2% of the control level at 9 days of storage at 8C
-
heat pretreatment at 38C for 3 days induces accumulation of PAL protein. During storage at 8C for 12 days, the amounts of PAL protein in peel tissues of control and heat-pretreated fruit increase, reaching a maximum after 9 days and finally decrease by 12 days of storage, the heat-pretreated banana fruit peel tissue is consistently stronger than that of the control fruit at any time during chilling storage
-
-80C, storage buffer, several months, no loss of activity
-
0-2C, rapid loss of PAL activity during storage of the yeast cells, Mn2+-dependent storage stabilization: whole cells retain nearly 85% of the original enzyme activity for at least 12 weeks with 0.01% Mn2+ in storage buffer containing 50 mM Tris-HCl, pH 8.8, while the control loses all enzyme activity after 8 weeks. Ca2+, Mg2+, Zn2+ or Li+ can only partially substitute for Mn2+, overview
-
-20C, PAL activity in freeze-dried wheat seedling tissues following three months of storage range from 62% in the leaf to 89% in root/residual seed tissues, after a 3 h two-stage in vitro digestion, 36% and 42% recovery of PAL activity is associated with chopped fresh leaf and root/residual seed tissues respectively, no activity is recovered from freeze-dried tissues
-
effects of freezing temperature on PAL activity of freeze-dried tissues, overview, -18C results in the best retention of PAL activity
Q43210
4C, 5% loss of activity after 1 week, 40% loss of activity after 1 month
-
22C, freeze-dried root material, approximately 67% loss of activity
Q8VXG7, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Alternaria sp.
-
-
P45724, P45725, Q9SS45
HiTrap affinity chromatography; Ni-IDA column column chromatography; recombinant protein from Escherichia coli
C0LL35
HiTrap Ni2+-chelating column chromatography
-
ammonium sulfate, DEAE-cellulose, Sephadex G-100, Q-Sepharose
-
enzyme form 1, 2 and 3
-
using the MagneHis protein purification system; using the MagneHis protein purification system; using the MagneHis protein purification system; using the MagneHis protein purification system
C6ZIA5, P25872, P35513, P45733
recombinant PAL
-
different enrichment methods
-
further 2fold purification of the commercial preparation by gel filtration
-
different enrichment methods
-
; different enrichment methods
-
different enrichment methods
-
3 isoenzymes: PAL-I, PAL-II and PAL-III
-
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
-, E3T9X0
expression in Escherichia coli
-
-
-, F4YRL1
-
P45724, P45725, Q9SS45
overexpression in Coleus blumei
P35510
-
D0E576
expressed in Pichia pastoris strain X-33
-
expressed in Pichia pastoris strain X-33 and Escherichia coli Top10 cells; expression in Escherichia coli and Pichia pastoris; expression in Escherichia coli an Pichia pastoris
C0LL35
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
-, C0LL35, D5KS97
DNA and amino acid sequence determination and analysis, primers designed from GenBank sequence D26596, UniProt ID P45726, semiquantitative expression analysis by RT-PCR
Q672H7
expression in Escherichia coli
D3Y5L6
gene pal1, genomic library screening, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis, recombinant expression in Escherichia coli strain XL1-Blue, identification of cis-acting regulatory DNA elements; gene pal2, genomic library screening, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis, recombinant expression in Escherichia coli strain XL1-Blue, identification of cis-acting regulatory DNA elements; gene pal3a, genomic library screening, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis, recombinant expression in Escherichia coli strain XL1-Blue, identification of cis-acting regulatory DNA elements; gene pal3b, genomic library screening, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis, recombinant expression in Escherichia coli strain XL1-Blue, identification of cis-acting regulatory DNA elements; gene pal4, genomic library screening, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis, recombinant expression in Escherichia coli strain XL1-Blue, identification of cis-acting regulatory DNA elements
B1GS29, B1GS31, B1GS33, -
transient expression of a loss-of-function mutant DcPAL3 promoter-reporter construct in protoplasts prepared from carrot suspension-cultured cells, both the GCC-box homolog and the box-L are required for overall DcPAL3 expression. Possible different mechanism in the normal and variant cultured cell lines, respectively, in terms DcPAL3 promoter regulation
B0M0P5, Q852S1
DNA and amino acid sequence determination, analysis, and comparison of PAL isozymes, expression and phylogenetic analysis
B5U983, -
gene GbPAL, DNA and amino acid sequence determination and analysis, the gene is intron-less and belongs to a small multi-gene family, expression analysis and sequence comparison
A7UHB6
expression in Escherichia coli
-, Q0GA81
expression in Escherichia coli
-
C- or N-terminal His-tagged enzymes are expressed in Escherichia coli Rosetta 2 (DE3) cells; C- or N-terminal His-tagged enzymes are expressed in Escherichia coli Rosetta 2 (DE3) cells; C- or N-terminal His-tagged enzymes are expressed in Escherichia coli Rosetta 2 (DE3) cells; C- or N-terminal His-tagged enzymes are expressed in Escherichia coli Rosetta 2 (DE3) cells
C6ZIA5, P25872, P35513, P45733
expression in Escherichia coli
-
expression in Escherichia coli
-
fusion proteins with gluthatione S-transferase expressed in Escherichia coli
-
expressed in Nicotiana tabacum
P52777
gene PALrs1, DNA and amino acid sequence determination and analysis, and analysis of egenomic structure, overview. Expression of PALrs1 under the 35S promoter with double-enhancer sequences from CaMV-W and TMV-W fragments in Rhodiola sachalinensis via Agrobacterium tumefaciens transfection method
Q5EIB6, -
expression in Escherichia coli
-
expression in Escherichia coli strain JM109
P11544
gene pal1, transcription profile, expression in Escherichia coli strain M15
A9XIW5
PAL genes, multi-gene family with about 26 copies in the diploid genome, DNA and amino acid sequence determination and analysis, distribution of PAL gene sequences in the tomato genome, overview, very active silencing suggesting aggressive competition between PAL gene duplication and copy inactivation during PAL gene evolution, expression analysis of isozymes in plants, overview. Expression in Escherichia coli strain DH5alpha
P35511
cloned into expression plasmid pHIS8. The recombinant EncP is overexpressed as an N-terminal octahistidyl-tagged fusion protein in Escherichia coli BL21
-
expression in Streptomyces lividans
-
the expression of genes PAL1 and PAL2, but not PAL3, is upregulated in transgenic cells expressing recombinant plant oncogene rolB of Agrobacterium rhizogenes, expression analysis, overview
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
increase in phenyl alanine ammonia lyase activity is observed at both the treatments of supplemental UV-B (pre-treatment of Psoralens against supplemental UV-B and supplemental UV-B) with maximum increment of 42.9% at pre-treatment of Psoralens against supplemental UV-B followed by 14.8% in supplemental UV-B as compared to the control at 20 days after germination
-
induced most strongly in response to 300 microM methyl jasmonate treatment at 6 h
-, F4YRL1
treatment of seedlings with 5 mM 3-aminobenzamide significantly reduces PAL activity in elf18-elicited seedlings
-
a 4fold increase of PAL activity is observed in chitosan-stimulated cell cultures (0.01 mg/ml) at 24 h post-elicitation
-
methyl jasmonate treatment during storage significantly inhibits the increase in activity of PAL
-
mRNA level of isoform PAL6 is higher in cultivar Camarosa than in cultivar Toyonoka
F8RL28
PAL activity increases after 48 h of incubation with ethephon at 22C and during fruit ripening
-
PAL mRNA level is higher in soybean roots growing in the presence of Cd2+ or Pb2+ than in the control. The highest amount of mRNA coding for PAL is observed in the presence of 15 mg/l of Cd2+ or 50 mg/l of Pb2+. The increase in activity is not directly correlated with the increase in mRNA
-
pretreatment of mycelia with 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide or aminoguanidine suppresses PAL activity
-
expression is induced by treatment with abscisic acid, gibberellin GA3, high and low temperature
-, Q0GA81
activities of polyphenol oxidase and PAL are highest after cultivation at low day/night temperatures of 20/13C, as is anthocyanin content
-
PAL mRNA level is lower in seedlings growing in the presence of Cd2+ than in the control
-
PAL mRNA level is higher in seedlings growing in the presence of Pb2+ than in the control. The increase in activity is not directly correlated with the increase in mRNA
-
transcript levels in leaves are significantly induced by methyl jasmonate, nitric oxide, and salicylic acid
B9VU66
PAL activity increases in both the leaf rosettes and the roots of Ni-treated chamomile (0.003-0.12 mM for 10 days)
-
0.25 mM salicylic acid sharply increases phenylalanine ammonia-lyase activity (24 h after application)
-
expression of PAL transcripts peak 4 h after exposure to 0.05 mg/ml yeast elicitor, whereas 0.025 mM methyl jasmonate induction of PAL transcripts is slower; expression of PAL transcripts peak 4 h after exposure to 0.05 mg/ml yeast elicitor, whereas 0.025 mM methyl jasmonate induction of PAL transcripts is slower; expression of PAL transcripts peak 4 h after exposure to 0.05 mg/ml yeast elicitor, whereas 0.025 mM methyl jasmonate induction of PAL transcripts is slower; expression of PAL transcripts peak 4 h after exposure to 0.05 mg/ml yeast elicitor, whereas 0.025 mM methyl jasmonate induction of PAL transcripts is slower
C6ZIA5, P25872, P35513, P45733
in riboflavin-treated inoculated plants, upregulation of PAL expression is detected downstream of lipoxygenase upregulation
-
Muktakeshi cultivar shows a higher increase in the PAL activity with the concentrations of the 0.0012 mg/l eliciting solution in the cell suspension culture medium
-
From 5 days post-anthesis to the onset of ripening PAL5 expression decreases gradually. PAL5 transcript level decreases after abscisic acid treatment (0.1 mM). Treatment with 10 mM H2O2 causes the PAL5 transcript level to decrease after 3 h, a similar decrease is observed for the PAL5 transcript after exposure to 0.05 mM methyl viologen for 3 h
P35511
in response to 200 mM NaCl and 200 mM mannitol treatment the PAL5 transcript increases significantly after 1 h of treatment and begins to decline gradually from then on
P35511
PAL activity of the 20-day-old immobilized Taxus cuspidata cells increases by 11% after 4 h treatment with 0.02 mM sodium nitroprusside
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C503S
-
site-directed mutagenesis
C503S/C565S
-
site-directed mutagenesis, structure analysis and comparison to the wild-type enzyme, the mutant shows increased activity and resistance to proteases compared to the wild-type enzyme
C503S/C565S
-
the mutant shows high protein stability and is very efficient as protein therapeutics in treatment of phenylketonuria, PKU, with lowered phenylalanine levels in both vascular space and brain tissue over a 90 day trial period, resulting in reduced manifestations associated with PKU, including reversal of PKU-associated hypopigmentation and enhanced animal health in a mouse model, the wild-type enzyme is less efective, overview
C565S
-
site-directed mutagenesis
L108A
-
slight decrease in catalytic activity
R91K
-
the mutant shows increased activity compared to the wild-type enzyme
F144H
-
decrease of activity with L-phenylalanine, increase of activity with L-tyrosine
F133H
-, C0LL35, D5KS97
decrease in ration kcat/KM value
L108A
-
slight decrease in catalytic activity
F137I
-
increased activity in the amination of p-nitro-cinnamic acid
F137T
-
increased activity in the amination of p-nitro-cinnamic acid
F137V
-
increased activity in the amination of p-nitro-cinnamic acid
L137H
-
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
V83A
-
mutant is more active than wild-type enzyme, turnover-number for L-Phe is 20.8fold higher than wild-type value, Km-value for L-Phe is 5.2fold higher than wild-type value
L108G
-
slight decrease in catalytic activity
additional information
-
mutant lacking 21 N-terminal amino acids, no adverse effects on catalytic activity
F134H
-, C0LL35, D5KS97
decrease in ratio kcat/KM value
additional information
B0M0P5, Q852S1
construction of a loss-of-function mutant DcPAL3 promoter-reporter construct and transient expression in protoplasts prepared from carrot suspension-cultured cells
L108G
-
slight decrease in catalytic activity
additional information
-
mutant lacking 21 N-terminal amino acids, no adverse effects on catalytic activity
L137H/Q487E
-
mutation almost doubles the kinetic D-isotope effect compared to wild-type enzyme
additional information
P24481
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
Y350F
-
kinetic D isotope effect is of the same magnitude as wild-type enzyme
additional information
-
building of Tyr-loop-in/loop-out model structure lacking the C-terminal domain
additional information
Q5EIB6, -
overexpression of the PALrs1 gene in Rhodiola sachalinensis plants results in a 3.3fold increase in 4-coumaric acid content, while levels of tyrosol and salidroside are 4.7fold and 7.7fold, respectively, lower in PALrs1 transgenic plants than in controls
additional information
-
activity PAL encapsulated in cellulose nitrate microcapsules is only 23% of the activity of PAL in Tris buffer due to its incomplete encapsulation, optimzation of encapsulation method and efficiency, method, PAL activity free in the aqueous core of the microcapsules is 85.7% of the total activity in the homogenate of the microcapsules, while the activity of PAL bound to the membrane of the microcapsules is 14.3% of the total activity in the homogenate of the microcapsules, overview
additional information
-
building of Tyr-loop-in/loop-out model structure lacking the C-terminal domain
V83H
-
inactive mutant
additional information
-
development of an encapsulation method and optimzation of enzyme stability, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pharmacology
-
the ability of PAL to catalyze the conversion of L-Phe into nontoxic compounds in the absence of additional cofactors leads to its use as a therapeutic agent for the treatment of phenylketonuria
agriculture
P35510
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
agriculture
-
PAL activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 24 hours after inoculation in the resistant varieties. Defense enzymes PAL, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. PAL is induced first, followed by tyrosine ammonia-lyase and than polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
agriculture
Camellia sinensis O. Kuntze
-
PAL activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 24 hours after inoculation in the resistant varieties. Defense enzymes PAL, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. PAL is induced first, followed by tyrosine ammonia-lyase and than polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
-
agriculture
-
treatment of plants with Pseudmonas sp. increases shoot length and significantly increases the activity of both peroxidase and phenylalanine ammonia-lyase. Treatment may help plants against pathogen invasion by modulating plant peroxidase and phenylalanine ammonia-lyase activities
agriculture
-
treatment of plants with Pseudomonas fluorescens and Pseudomonas aeruginosa induces enzyme synthesis associated with increased synthesis of phenolic compounds such as tannic, gallic, caffeic, chlorogenic and cinnamic acids. Treatment with Sclerotinia slerotiorum does not induce enzyme synthesis
agriculture
F8RL28
expression of isoform PAL6 is fruit-specific, and increases during fruit ripening in both cultivars along with anthocyanin accumulation. PAL enzyme activity increases at similar rates in both cultivars at early ripening stages, but at the end of ripening PAL activity diminishes in cultivar Toyonoka while it rises markedly in cultivar Camarosa. PAL activity is higher in internal fruit tissue, showing no correlation with anthocyanin level of the same section in both cultivars. The higher FaPAL6 expression and activity detected in Camarosa may be associated to the enhanced anthocyanin accumulation found in this cultivar
analysis
-
useful for determining Phe or removing Phe from mammalian systems
agriculture
-
during culture of Morinda citrifolia adventitious roots in different strength, i.e. 0.25, 0.50, 0.75, 1.0, 1.5 and 2.0 of Murashige and Skoog medium supplemented with 5 mg/l indole butyric acid and 30 g/l sucrose, phenylalanine ammonia lyase activity shows a positive correlation in relation to salt strength that leads to an increase in phenol biosynthesis in expense of anthraquinone formation. With the increasing salt strength, root growth and anthraquinone accumulation decrease significantly
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
agriculture
A0MQ91, -
level of enzyme mRNA increases 5 days after the establishment of in vitro callus unions. Enzyme transcription shows a higher level in graft union of incompatible partners and does not result in formation of lignin
agriculture
A0MQ92
level of enzyme mRNA increases 5 days after the establishment of in vitro callus unions. Enzyme transcription shows a higher level in graft union of incompatible partners and does not result in formation of lignin
synthesis
Q5EIB6, -
the enzyme is involved in and useful for production salidroside, an effective adaptogenic drug from the medicinal plant Rhodiola sachalinensis
synthesis
Rhodococcus rubra
-
production of L-phenylalanine, which is used in the manufacture of the artificial sweetener aspartame and in parenteral nutrition, it is also used as a building block for the synthesis of the macrolide antibiotic rutamycin B
medicine
-
use of enzyme for substitution treatment of human phenylketonuria. Identification of B and T cell epitopes on the enzyme protein and covering of the immunogenic regions
synthesis
-
improvement of recombinant phenylalanine ammonia-lyase stability in Escherichia coli during the enzymatic methods of L-phenylalanine production. The optimum values for testing variables are 13.04 mM glycerol, 1.87 mM sucrose, 4.09 mM DTT, and 69 mM Mg2+. The maximum phenylalanine ammonia-lyase activity is retained as 67.73 units/g after three successive cycles of bioconversion. In comparison to initial phenylalanine ammonia-lyase activity, the loss of phenylalanine ammonia-lyase activity was only 22%. Phenylalanine ammonia-lyase activity is enhanced about 23% in comparison to the control
analysis
-
immobilization of phenylalanine ammonia-lyase into gelatin on polyester films to determine phenylalanine in urine for the prediagnosis of phenylketonuria. Immobilized enzyme retaines 100% apparent activity after 30 days and as much as 75% of activity is retained after 2 months. The method is sufficiently sensitive to determine the phenylalanine concentration in phenylketonuric infants' urine
medicine
-
use of enzyme in therapy of human phenylketonuria. Preparation of microcapsules containing emulsified enzyme. Emulsification of enzyme solution with water-saturated ether causes no loss in activity but results in loss of protein content in the aqueous phase due to specific loss of impurities in the protein sample. Emulsification of enzyme solution with ether/ethanol mixture results in a 50% decrase in activity. Hydroxypropyl-gamma-cyclodextrin and hydroxypropyl-beta-cyclodextrin protect against emulsion mediated loss in activity
synthesis
-
phenylalanine ammonia-lyase's reverse reaction is exploited for the commercial production of optically pure L-phenylalanine from trans-cinnamic acid
synthesis
-
the enzyme is useful for an economic way for biosynthesis of 15NL-phenylalanine, yield and purity of 15NL-phenylalanine reach 71% and 99.3%, respectively
synthesis
Rhodotorula glutinis AS2.102
-
the enzyme is useful for an economic way for biosynthesis of 15NL-phenylalanine, yield and purity of 15NL-phenylalanine reach 71% and 99.3%, respectively
-
synthesis
Rhodotorula glutinis RE4607095D
-
phenylalanine ammonia-lyase's reverse reaction is exploited for the commercial production of optically pure L-phenylalanine from trans-cinnamic acid
-
synthesis
-
production of L-phenylalanine, which is used in the manufacture of the artificial sweetener aspartame and in parenteral nutrition, it is also used as a building block for the synthesis of the macrolide antibiotic rutamycin B
agriculture
-
treatment of plants with Pseudmonas sp. increases shoot length and significantly increases the activity of both peroxidase and phenylalanine ammonia-lyase. Treatment may help plants against pathogen invasion by modulating plant peroxidase and phenylalanine ammonia-lyase activities
synthesis
-
heterologous expression of enzyme in Streptomyces lividans. After 4 days of cultivation using glucose as carbon source, the maximal level of cinnamic acid reaches 210 mg/l. When glycerol is used as carbon source az 30 g/l, the maximal level of produced cinnamic acid reaches 450 mg/l. Using raw starch, xylose or xylan as carbon source, the maximal level of cinnamic acid reaches 460, 300, and 130 mg/l, respectively
medicine
-
the enzyme can be used as oral therapeutic, in an encapsulated form, in phenylketonuria/hyperphenylalaninemia
medicine
Q43210
PAL activity is able to effect a reduction in phenylalanine levels and hence provide the basis of a unique therapy for human hyperphenylalaninemic patients