Information on EC 4.3.1.23 - tyrosine ammonia-lyase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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 ACCESSION NO.
LITERATURE
L-tyrosine = trans-p-hydroxycinnamate + NH3
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
coumarins biosynthesis (engineered)
-
naringenin biosynthesis (engineered)
-
Phenylpropanoid biosynthesis
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
TAL
-
-
tyrosine ammonia lyase
-
-
tyrosine ammonia lyase
-
-
tyrosine ammonia lyase
-
-
tyrosine ammonia-lyase
-
-
tyrosine ammonia-lyase
-
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
O. Kuntze
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
-
?
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
-
assay at 40C
-
-
?
L-tyrosine
trans-p-hydroxycinnamate + NH3
show the reaction diagram
-
assay at 40C, pH 7.8
-
-
?
L-tyrosinol
?
show the reaction diagram
-
-
-
-
?
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-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
-
-
-
r
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
S-methyl 1,2,3-benzothiadiazole-7-carbothioate
-
treatment of fruits
additional information
-
higher activity in seedlings treated with humic substances
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.28
-
L-phenylalanine
-
35C, pH 9.4
2.7
-
L-phenylalanine
-
-
0.016
-
L-tyrosine
-
35C, pH 8.5
0.1
-
L-tyrosine
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.226
-
L-phenylalanine
-
-
12364
10
-
L-tyrosine
-
-
12450
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.8
-
-
assay at
8.5
-
-
deaminantion of L-tyrosine
9.4
-
-
deaminantion of L-phenylalanine
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
assay at
40
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombiannt TAL
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
overexpression in Arabidopsis thaliana
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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
-