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 hide
4.3.1.23
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RECOMMENDED NAME
GeneOntology No.
tyrosine ammonia-lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-tyrosine = trans-p-hydroxycinnamate + NH3
show the reaction diagram
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
O. Kuntze
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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catalyzes first commited step in the biosynthesis of phenolics
physiological function
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
trans-cinnamate + NH3
show the reaction diagram
L-tyrosine
p-hydroxycinnamic acid + NH3
show the reaction diagram
-
-
-
?
L-tyrosine
trans-p-hydroxycinnamate + NH3
show the reaction diagram
L-tyrosinol
?
show the reaction diagram
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-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-phenylalanine
trans-cinnamate + NH3
show the reaction diagram
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-
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r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
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activity: 82%, crude: 100%
CuSO4
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activity: 46%, crude: 100%
FeCl3
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activity: 58%, crude: 100%
MgSO4
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activity: 72%, crude: 100%
MnSO4
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activity: 46%, crude: 100%
Na2MoO4
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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 hide
LITERATURE
IMAGE
S-methyl 1,2,3-benzothiadiazole-7-carbothioate
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treatment of fruits
additional information
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higher activity in seedlings treated with humic substances
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.28 - 2.7
L-phenylalanine
0.016 - 0.1
L-tyrosine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 15.1
L-phenylalanine
0.9 - 27.7
L-tyrosine
0.12
L-tyrosinol
Rhodobacter sphaeroides
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.226
L-phenylalanine
Rhodobacter sphaeroides
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104
10
L-tyrosine
Rhodobacter sphaeroides
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109
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00013
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seedling without treatment with humic substances
0.00075
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seedlings treated with 2 mg C/l of humic substances
additional information
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80.3 U/mg protein, 1 unit is defined as the amount of enzyme causing an increase in absorbtion
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
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assay at
8.5
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deaminantion of L-tyrosine
8.9
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assay at
9.4
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deaminantion of L-phenylalanine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10.5
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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 hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
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
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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 hide
LITERATURE
agriculture