Information on EC 4.3.1.23 - tyrosine ammonia-lyase

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

EC NUMBER
COMMENTARY
4.3.1.23
-
RECOMMENDED NAME
GeneOntology No.
tyrosine ammonia-lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tyrosine = trans-p-hydroxycinnamate + NH3
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
coumarins biosynthesis (engineered)
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naringenin biosynthesis (engineered)
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Tyrosine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-tyrosine ammonia-lyase (trans-p-hydroxycinnamate-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), EC 4.3.1.24 (phenylalanine 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 [1]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [3]. The enzyme is far more active with tyrosine than with phenylalanine as substrate, but the substrate specificity can be switched by mutation of a single amino acid (H89F) in the enzyme from the bacterium Rhodobacter sphaeroides [1,2].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TAL
-
-
tyrosine ammonia lyase
-
-
tyrosine ammonia lyase
-
-
tyrosine ammonia lyase
-
-
tyrosine ammonia lyase
-
-
tyrosine ammonia-lyase
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-
tyrosine ammonia-lyase
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-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
O. Kuntze
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
catalyzes first commited step in the biosynthesis of phenolics
physiological function
-
tyrosine ammonia-lyase activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 48 hours after inoculation in the resistant varieties. Defense enzymes phenylalanine ammonia-lyase, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. Phenylalanine ammonia-lyase is induced first, followed by tyrosine ammonia-lyase and then polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
physiological function
Camellia sinensis O. Kuntze
-
tyrosine ammonia-lyase activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 48 hours after inoculation in the resistant varieties. Defense enzymes phenylalanine ammonia-lyase, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. Phenylalanine ammonia-lyase is induced first, followed by tyrosine ammonia-lyase and then polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
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SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
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-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
?, r
L-tyrosine
p-hydroxycinnamic acid + NH3
show the reaction diagram
-
-
-
?
L-tyrosine
trans-p-hydroxycinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-tyrosine
trans-p-hydroxycinnamate + NH3
show the reaction diagram
-
-
-
-
?
L-tyrosine
trans-p-hydroxycinnamate + NH3
show the reaction diagram
-
assay at 40C
-
-
?
L-tyrosine
trans-p-hydroxycinnamate + NH3
show the reaction diagram
-
assay at 40C, pH 7.8
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-
?
L-tyrosinol
?
show the reaction diagram
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-
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?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CaCl2
-
activity: 82%, crude: 100%
CuSO4
-
activity: 46%, crude: 100%
FeCl3
-
activity: 58%, crude: 100%
MgSO4
-
activity: 72%, crude: 100%
MnSO4
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activity: 46%, crude: 100%
Na2MoO4
-
activity: 58%, crude: 100%
NiSO4
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activity: 115%, crude: 100%
ZnSO4
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activity: 43%, crude: 100%
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-methyl 1,2,3-benzothiadiazole-7-carbothioate
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treatment of fruits
additional information
-
higher activity in seedlings treated with humic substances
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.28
L-phenylalanine
-
35C, pH 9.4
2.7
L-phenylalanine
-
-
0.016
L-tyrosine
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35C, pH 8.5
0.1
L-tyrosine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
L-phenylalanine
-
-
15.1
L-phenylalanine
-
35C, pH 9.4
0.9
L-tyrosine
-
-
27.7
L-tyrosine
-
35C, pH 8.5
0.12
L-tyrosinol
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.226
L-phenylalanine
-
-
104
10
L-tyrosine
-
-
109
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00013
-
seedling without treatment with humic substances
0.00075
-
seedlings treated with 2 mg C/l of humic substances
additional information
-
80.3 U/mg protein, 1 unit is defined as the amount of enzyme causing an increase in absorbtion
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
-
assay at
8.5
-
deaminantion of L-tyrosine
8.9
-
assay at
9.4
-
deaminantion of L-phenylalanine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10.5
-
deamination of L-tyrosine, approx. 14% of maximal activity at pH 6.0, approx. 20% of maximal activity at pH 10.5, deaminantion of L-phenylalanine, approx. 1% of maximal activity at pH 6.0, approx. 75% of maximal activity at pH 10.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
assay at
40
-
assay at
40
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombiannt TAL
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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overexpression in Arabidopsis thaliana
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
tyrosine ammonia-lyase activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 48 hours after inoculation in the resistant varieties. Defense enzymes phenylalanine ammonia-lyase, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. Phenylalanine ammonia-lyase is induced first, followed by tyrosine ammonia-lyase and then polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
agriculture
Camellia sinensis O. Kuntze
-
tyrosine ammonia-lyase activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 48 hours after inoculation in the resistant varieties. Defense enzymes phenylalanine ammonia-lyase, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. Phenylalanine ammonia-lyase is induced first, followed by tyrosine ammonia-lyase and then polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
-