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Information on EC 4.3.1.24 - phenylalanine ammonia-lyase and Organism(s) Nicotiana tabacum and UniProt Accession P25872

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.24 phenylalanine ammonia-lyase
IUBMB Comments
This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase) and EC 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family . This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine . The enzyme from some species is highly specific for phenylalanine [7,8].
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Nicotiana tabacum
UNIPROT: P25872
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The taxonomic range for the selected organisms is: Nicotiana tabacum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phenylalanine ammonia-lyase, phenylalanine ammonia lyase, l-phenylalanine ammonia-lyase, dcpal1, phe ammonia-lyase, rgpal, avpal, palrs1, atpal2, sspal1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-phenylalanine ammonia-lyase
-
L-phenylalanine ammonia-lyase
-
SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine ammonia-lyase (trans-cinnamate-forming)
This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase) and EC 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family [3]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [9]. The enzyme from some species is highly specific for phenylalanine [7,8].
CAS REGISTRY NUMBER
COMMENTARY hide
9024-28-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-phenylalanine
(E)-cinnamate + NH3
show the reaction diagram
-
-
-
?
L-Phe
(E)-cinnamate + NH3
show the reaction diagram
L-phenylalanine
(E)-cinnamate + NH3
show the reaction diagram
-
-
-
?
L-tyrosine
p-coumarate + NH3
show the reaction diagram
-
no activity
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
competitive inhibition
2-mercaptoethanol
competitive inhibition
CN-
-
irreversible
NaBH4
-
irreversible
o-coumarate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0598
L-phenylalanine
isoform PAL1, at 30°C in 50 mM Tris/HCl, pH 8.5
0.011 - 0.22
L-Phe
0.0364 - 0.0524
L-phenylalanine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.09
L-phenylalanine
isoform PAL1, at 30°C in 50 mM Tris/HCl, pH 8.5
0.78 - 1.53
L-phenylalanine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.28
L-phenylalanine
isoform PAL1, at 30°C in 50 mM Tris/HCl, pH 8.5
21.1 - 29.09
L-phenylalanine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
2-mercaptoethanol
isoform PAL1
3
2-mercaptoethanol
isoform PAL1
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.6
-
-
8.8
-
tissue culture
8.8 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
isoform PAL1 with His-tag, isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform PAL1; cultivar Xanthi
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
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
-
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
L-phenylalanine ammonia-lyase is the first enzyme of phenylpropanoid biosynthesis
metabolism
L-phenylalanine ammonia-lyase is the first enzyme of phenylpropanoid biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PAL1_TOBAC
715
0
77781
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
262000
PAL1 with a C-terminal His-tag, gel filtration
70000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
4 * 70000
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, storage buffer, several months, no loss of activity
-80°C, storage buffer, several months, no loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using the MagneHis protein purification system
using the MagneHis protein purification system
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Camm, E.L.; Towers, G.H.N.
Phenylalanine ammonia lyase
Phytochemistry
12
961-973
1973
Avena sativa, Hordeum vulgare, Ipomoea batatas, Nicotiana tabacum, Pisum sativum, Pteridium aquilinum, Quercus pedunculata, Rhodotorula glutinis, Rhodotorula texensis, Solanum tuberosum, Sporobolomyces roseus, Streptomyces verticillatus, Tulipa hybrid cultivar, Ustilago hordei
-
Manually annotated by BRENDA team
Nagai, N.; Kojima, Y.; Shimosaka, M.; Okazaki, M.
Effects of kinetin on L-phenylalanine ammonia-lyase activity in tobacco cell culture
Agric. Biol. Chem.
52
2617-2619
1988
Nicotiana tabacum
-
Manually annotated by BRENDA team
Achnine, L.; Blancaflor, E.B.; Rasmussen, S.; Dixon, R.A.
Colocalization of L-phenylalanine ammonia-lyase and cinnamate 4-hydroxylase for metabolic channeling in phenylpropanoid biosynthesis
Plant Cell
16
3098-3109
2004
Nicotiana tabacum
Manually annotated by BRENDA team
Reichert, A.I.; He, X.Z.; Dixon, R.A.
Phenylalanine ammonia-lyase (PAL) from tobacco (Nicotiana tabacum): characterization of the four tobacco PAL genes and active heterotetrameric enzymes
Biochem. J.
424
233-242
2009
Nicotiana tabacum (C6ZIA5), Nicotiana tabacum (P25872), Nicotiana tabacum (P35513), Nicotiana tabacum (P45733), Nicotiana tabacum
Manually annotated by BRENDA team