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Information on EC 2.6.1.5 - tyrosine transaminase
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EC Tree
2.6.1.5 tyrosine transaminaseIUBMB Comments
A pyridoxal-phosphate protein. L-Phenylalanine can act instead of L-tyrosine. The mitochondrial enzyme may be identical with EC 2.6.1.1 (aspartate transaminase). The three isoenzymic forms are interconverted by EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain). The enzyme can also catalyse the final step in the methionine-salvage pathway of Klebsiella pneumoniae .
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Word Map
- 2.6.1.5
- glucocorticoid
- dexamethasone
- hepatoma
- hepatocytes
- steroid
- insulin
- albumin
- glucagon
-
liver-specific
-
adrenalectomized
- hydrocortisone
- corticosterone
- fetal
- alpha-fetoprotein
- oxygenase
- glycogen
- phosphoenolpyruvate
-
carboxykinase
- tyrosinemia
- camp
- ornithine
-
transamination
-
gluconeogenesis
-
dibutyryl
- cortisol
-
pyrrolase
- pyridoxal
-
antiglucocorticoids
- aminotransferases
- glucose-6-phosphatase
-
glucocorticoid-induced
- pepck
-
gluconeogenic
-
reuber
-
morris
-
hepatocyte-specific
-
dexamethasone-induced
- methylprednisolone
-
bt2camp
- dex
-
glucocorticoid-responsive
- triamcinolone
- p-hydroxyphenylpyruvate
-
rosmarinic
-
acetonide
-
hepatocyte-like
-
palmoplantar
-
hyperkeratosis
-
glucocorticoid-dependent
- medicine
-
superinduction
The enzyme appears in viruses and cellular organisms
Synonyms
aminotransferase, tyrosine, At5g36160, At5g53970, beta-phenylalanine aminotransferase, glutamic phenylpyruvic aminotransferase, glutamic-hydroxyphenylpyruvic transaminase, L-phenylalanine 2-oxoglutarate aminotransferase, L-tyrosine aminotransferase, L-tyrosine-2-oxoglutarate aminotransferase, More, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminotransferase, tyrosine
-
-
-
-
glutamic phenylpyruvic aminotransferase
-
-
-
-
glutamic-hydroxyphenylpyruvic transaminase
-
-
-
-
L-phenylalanine 2-oxoglutarate aminotransferase
-
-
-
-
L-tyrosine aminotransferase
-
-
-
-
L-tyrosine-2-oxoglutarate aminotransferase
-
-
-
-
phenylalanine aminotransferase
-
-
-
-
phenylalanine transaminase
-
-
-
-
phenylalanine-alpha-ketoglutarate transaminase
-
-
-
-
phenylpyruvate transaminase
-
-
-
-
phenylpyruvic acid transaminase
-
-
-
-
TAT
TyrAT
tyrosine aminotransferase
tyrosine-2-ketoglutarate aminotransferase
-
-
-
-
tyrosine-2-oxoglutarate aminotransferase
-
-
-
-
tyrosine-alpha-ketoglutarate aminotransferase
-
-
-
-
tyrosine-alpha-ketoglutarate transaminase
-
-
-
-
additional information
-
the mitochondrial enzyme may be identical with EC 2.6.1.1 and with EC 2.6.1.57
tyrosine aminotransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
Biosynthesis of secondary metabolites, Cysteine and methionine metabolism, Isoquinoline alkaloid biosynthesis, Novobiocin biosynthesis, Phenylalanine metabolism, Phenylalanine, tyrosine and tryptophan biosynthesis, Tropane, piperidine and pyridine alkaloid biosynthesis, Tyrosine metabolism, Ubiquinone and other terpenoid-quinone biosynthesis
MetaCyc
(S)-reticuline biosynthesis I, 4-hydroxybenzoate biosynthesis I (eukaryotes), 4-hydroxyphenylpyruvate biosynthesis, atromentin biosynthesis, L-tyrosine biosynthesis I, L-tyrosine degradation I, L-tyrosine degradation II, L-tyrosine degradation III, L-tyrosine degradation IV (to 4-methylphenol), L-tyrosine degradation V (Stickland reaction), rosmarinic acid biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
L-tyrosine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. L-Phenylalanine can act instead of L-tyrosine. The mitochondrial enzyme may be identical with EC 2.6.1.1 (aspartate transaminase). The three isoenzymic forms are interconverted by EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain). The enzyme can also catalyse the final step in the methionine-salvage pathway of Klebsiella pneumoniae [8].
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CAS REGISTRY NUMBER
COMMENTARY
9014-55-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2-aminophenyl)alanine + 2-oxoglutarate
3-(4-aminophenyl)-2-oxopropanoate + L-glutamate
-
10% of the activity that with L-tyrosine
-
?
(3-fluorophenyl)alanine + 2-oxoglutarate
3-(3-fluorophenyl)-2-oxopropanoate + L-glutamate
-
4% of the activity that with L-tyrosine
-
?
(4-chlorophenyl)alanine + 2-oxoglutarate
3-(3-chlorophenyl)-2-oxopropanoate + L-glutamate
-
17% of the activity with L-tyrosine
-
?
(4-fluorophenyl)alanine + 2-oxoglutarate
3-(4-fluorophenyl)-2-oxopropanoate + L-glutamate
-
7.9% of the activity that with L-tyrosine
-
?
(R)-3-amino-5-methyl-hexanoic acid + 2-oxoglutarate
?
relative activity: 48%
-
-
?
(S)-beta-phenylalanine + 2-oxoglutarate
3-oxo-3-phenylpropionic acid + L-glutamate
relative activity: 100%
-
-
?
(S)-beta-phenylalanine + pyruvate
3-oxo-3-phenylpropionic acid + L-alanine
the activity of VpAT with pyruvate is 85% of that with alpha-ketoglutarate as the amino acceptor
-
-
?
2-oxoglutarate + L-phenylalanine
L-glutamate + phenylpyruvate
-
-
-
?
3,4-dihydroxyphenylalanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
L-tyrosine + 2-oxoglutarate
-
-
-
r
3-aminotyrosine + 2-oxoglutarate
3-(3-amino-4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
-
16% of the activity than with L-tyrosine
-
?
3-methoxytyrosine + 2-oxoglutarate
3-(3-methoxy-4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
-
22% of the activity with L-tyrosine
-
?
4-hydroxyphenylpyruvate + L-aspartate
L-tyrosine + oxaloacetate
-
35% of the activity with L-glutamate
-
r
4-hydroxyphenylpyruvate + L-phenylalanine
L-glutamate + phenylpyruvate
-
-
-
?
L-asparagine + 2-oxoglutarate
2-oxosuccinamate + L-glutamate
-
15% of the activity with L-tyrosine
-
?
L-cysteine + 2-oxoglutarate
3-mercapto-2-oxopropanoate + L-glutamate
-
higher activity than with L-tyrosine
-
?
L-ethionine + 2-oxoglutarate
4-ethylsulfanyl-2-oxobutanoate + L-glutamate
-
17% of the activity than with L-tyrosine
-
?
L-glutamate + phenylpyruvate
2-oxoglutarate + L-phenylalanine
-
-
-
r
L-tryptophan + 2-oxoglutarate
3-(1H-indol-3-yl)-2-oxopropanoate + L-glutamate
-
-
-
-
?
L-tryptophan + oxaloacetate
3-(1H-indol-3-yl)-2-oxopropanoate + L-glycine
-
-
-
-
?
L-tryptophan + pyruvate
3-(1H-indol-3-yl)-2-oxopropanoate + L-alanine
-
-
-
-
?
L-tyrosine + 2-oxohexanoate
3-(4-hydroxyphenyl)-2-oxopropanoate + (2S)-2-aminohexanoate
-
-
-
-
?
L-tyrosine + 2-oxopentanoate
3-(4-hydroxyphenyl)-2-oxopropanoate + (2S)-2-aminopentanoate
relative activity compared to 2-oxoglutarate: 3%
-
-
?
L-tyrosine + oxaloacetate
?
relative activity compared to 2-oxoglutarate: 75%
-
-
?
L-tyrosine + phenylpyruvate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-phenylalanine
-
-
-
-
?
L-tyrosine + phenylpyruvate
4-hydroxyphenylpyruvate + L-phenylalanine
-
-
-
r
L-tyrosine + prephenate
?
relative activity compared to 2-oxoglutarate: 23%
-
-
?
L-tyrosine + pyruvate
?
relative activity compared to 2-oxoglutarate: 40%
-
-
?
rac-2-fluoro-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 15%
-
-
?
rac-2-methyl-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 5%
-
-
?
rac-3-bromo-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 53%
-
-
?
rac-3-chloro-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 56%
-
-
?
rac-3-fluoro-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 48%
-
-
?
rac-3-methyl-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 54%
-
-
?
rac-4-bromo-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 62%
-
-
?
rac-4-ethyl-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 134%
-
-
?
rac-4-fluoro-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 87%
-
-
?
rac-4-iso-propyl-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 61%
-
-
?
rac-4-methyl-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 100%
-
-
?
rac-4-nitro-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 32%
-
-
?
rac-4-nitro-hydroxy-phenylalanine + 2-oxoglutarate
?
relative activity: 61%
-
-
?
rac-4-propyl-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 126%
-
-
?
rac-4-trifluoromethyl-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 73%
-
-
?
rac-beta-phenylalanine + 2-oxoglutarate
?
relative activity: 100%
-
-
?
3,4-dihydroxyphenylalanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
-
-
-
?
3,4-dihydroxyphenylalanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
-
85% of the activity than with L-tyrosine
-
?
3-iodotyrosine + 2-oxoglutarate
3-(4-hydroxy-3-iodophenyl)-2-oxopropanoate + L-glutamate
-
as effective as L-tyrosine
-
?
3-iodotyrosine + 2-oxoglutarate
3-(4-hydroxy-3-iodophenyl)-2-oxopropanoate + L-glutamate
-
84% of the activity than with L-tyrosine
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
isoenzymes TAT-2 and TAT-3, best substrate for isoenzyme TAT-3
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
higher activity than with L-tyrosine
-
?
L-glutamate + 4-hydroxyphenylpyruvate
2-oxoglutarate + L-tyrosine
-
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
20% of the activity than with L-tyrosine
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropanoate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropanoate + L-glutamate
-
-
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropanoate + L-glutamate
-
-
-
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
lower activity than with L-tyrosine
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
higher rate than with L-tyrosine
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
no activity
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
best substrate
-
-
r
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
highly specific for: L-tyrosine
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
isoenzymes TAT-1, TAT-2 and TAT-3 show a pronounced preference for L-tyrosine over other aromatic amino acids
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
isoenzyme TAT-1: oxaloacetate and 2-oxoglutarate utilized equally well as amino acceptor, isoenzyme TAT-2: oxaloacetate is most effective, isoenzyme TAT-3: 2-oxoglutarate is most effective
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
first step in tyrosine pathway leading to the formation of rosmarinic acid (alpha-O-caffeoyl-3,4-dihydroxyphenyllactic acid)
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
specific for 2-oxoglutarate as the amino group acceptor
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
r
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
maximal activity with L-tyrosine
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
highly specific for: L-tyrosine
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
?
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
-
-
-
?
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
-
-
-
?
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
-
no activity
-
?
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
-
-
-
r
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
-
no activity
-
?
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
-
-
-
?
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
-
-
-
?
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
-
-
-
?
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
-
62% of the activity than with L-tyrosine
-
?
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
-
no activity
-
-
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
-
-
-
-
-
additional information
?
-
-
no detectable transamination of aspartate or other cosubstrates
-
-
-
additional information
?
-
-
leishmanial TAT is deprived of ALAT activity and exhibits undetectable activity towards leucine, glutamine and cysteine, leishmanial TAT reveals undetectable activity when other 2-oxoacids such as 2-oxoglutarate, glyoxylate, 2-oxoisovalerate and 2-oxoisocaproate are assayed at a concentration up to 10 mM, the leishmanial enzyme displays almost identical preference for 2-oxo-4-methylthiobutyrate, pyruvate and 2-oxobutyrate
-
-
-
additional information
?
-
activities with glutamate, methionine and leucine do not exceed 13% of the activity with tyrosine. Only phenylpyruvate and 2-oxoglutarate effectively serve as acceptors, and no activity is detected with prephenate
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
first step in tyrosine pathway leading to the formation of rosmarinic acid (alpha-O-caffeoyl-3,4-dihydroxyphenyllactic acid)
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
relative position of the cofactor at the active site determined by X-ray crystallography
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Hg2+
-
a dose of 1-3 mg/kg increases the basal activity of the enzyme and decreases its induction by dexamethasone
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4-hydroxyphenyl)acetic acid
-
74% inhibition with tyrosine at 3 mM and (4-hydroxyphenyl)acetic acid at 12 mM
2-chloro-3-(5-{[(2,6-difluorobenzyl)oxy]methyl}-5-methyl-4,5-dihydro-1,2-oxazol-3-yl)-6-(propan-2-yl)pyridine
-
1 mM: 79% inhibition of enzyme activity, 0.5 mM: 67% inhibition of enzyme activity, 0.25 mM: 44% inhibition of enzyme activity
3,4-Dihydroxyphenyllactate
-
strong inhibition of all the three TAT isoenzymes
3-(5-{[(2,6-difluorobenzyl)oxy]methyl}-5-methyl-4,5-dihydro-1,2-oxazol-3-yl)pyridine-2-carbonitrile
-
1 mM: 82% inhibition of enzyme activity, 0.5 mM: 46% inhibition of enzyme activity, 0.25 mM: 8% inhibition of enzyme activity
4-methylsulfonyl-2,5,6,2',4',5'-hexachlorobiphenyl
-
significant reduction of dexamethasone-induced activity, 50% inhibition at 0.0008 mM
4-methylsulfonyl-2,5,6,2',4'-pentachlorobiphenyl
-
significant reduction of dexamethasone-induced activity, 50% inhibition at 0.0007 mM
5-hydroxyindole acetic acid
-
55% inhibition with tyrosine at 3 mM and 5-hydroxyindole acetic acid at 12 mM
5-hydroxytryptophan
-
30% inhibition with tyrosine at 3 mM and 5-hydroxytryptophan at 12 mM
alpha-Methyl-L-aspartate
-
with L-tyrosine and 2-oxoglutarate or oxaloacetate as substrates
beta-Methyl-L-aspartate
-
with L-tyrosine and 2-oxoglutarate or oxaloacetate as substrates
cinmethylin
-
0.5 mM: 96% inhibition of enzyme activity, 0.25 mM: 20% inhibition of enzyme activity
Dextran sulfate
-
dextran sulfate inhibits TAT activity but conditioned macrophage medium reliably increases enzyme activity in hepatocytes
-
dihydroxymandelic acid
-
65% inhibition with tyrosine at 3 mM and dihydroxymandelic acid at 3 mM
dihydroxyphenylacetic acid
-
88% inhibition with tyrosine at 3 mM and dihydroxyphenylacetic acid at 3 mM
indole-3-acetic acid
-
42% inhibition with tyrosine at 3 mM and indole-3-acetic acid at 12 mM
indole-3-butyric acid
-
71% inhibition with tyrosine at 3 mM and indole-3-butyric acid at 12 mM
Indole-3-propionic acid
-
48% inhibition with tyrosine at 3 mM and indole-3-propionic acid at 12 mM
ketoconazole
-
significant reduction of dexamethasone-induced activity, 50% inhibition at 0.0011 mM
L-aspartate
-
with L-tyrosine and 2-oxoglutarate or oxaloacetate as substrates
methiozolin
-
0.5 mM: 91% inhibition of enzyme activity, 0.25 mM: 57% inhibition of enzyme activity
phenylacetic acid
-
30% inhibition with tyrosine at 3 mM and phenylacetic acid at 12 mM
Phenylethylamine
-
80% inhibition with tyrosine at 3 mM and phenylethylamine at 12 mM
tolylfluanid
-
significant reduction of dexamethasone-induced activity, 50% inhibition at 0.0014 mM
vanillylmandelic acid
-
51% inhibition with tyrosine at 3 mM and vanillylmandelic acid at 3 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adrenaline
-
activation is independent of the concentration of tyrosine, maximal activation achieved with 7-10 micromolar of adrenaline
dexamethasone
-
dexamethasone (5 mg) induces a significant increase in TAT activity, a further increase in TAT activity is not observed in the hepatocytes from the deficient rats, in contrast to the cells from the controls, when glucagon is added simultaneously with dexamethasone
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.9
4-hydroxyphenylpyruvate
cosubstrate phenylalanine, pH 10.0, 30°C
4.3
L-phenylalanine
cosubstrate 4-hydroxyphenylpyruvate, pH 10.0, 30°C
0.21
L-tyrosine
-
aspartate aminotransferase with mutations HEX and I73V, A293D, pH 8.0, 25°C
0.29
L-tyrosine
-
aspartate aminotransferase with mutations HEX and I73V, pH 8.0, 25°C
0.33
L-tyrosine
-
aspartate aminotransferase with mutations HEX and A293D, pH 8.0, 25°C
1.2
p-hydroxyphenylpyruvate
mutant R315K, pH 7.5, 37°C; wild-type, pH 7.5, 37°C
additional information
additional information
-
non-Michaelis complex kinetic
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
4-hydroxyphenylpyruvate
cosubstrate phenylalanine, pH 10.0, 30°C
0.17
L-phenylalanine
cosubstrate 4-hydroxyphenylpyruvate, pH 10.0, 30°C
25.6
L-tyrosine
-
aspartate aminotransferase with mutations HEX and I73V, pH 8.0, 25°C
35.7
L-tyrosine
-
aspartate aminotransferase with mutations HEX and I73V, A293D, pH 8.0, 25°C
39
L-tyrosine
-
aspartate aminotransferase with mutations HEX and A293D, pH 8.0, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
4-hydroxyphenylpyruvate
cosubstrate phenylalanine, pH 10.0, 30°C
0.04
L-phenylalanine
cosubstrate 2-oxoglutarate, pH 10.0, 30°C; cosubstrate 4-hydroxyphenylpyruvate, pH 10.0, 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
82.4
2-oxoglutarate
enzyme shows substrate inhibition, pH 7.6, 30°C
40.3
beta-phenylalanine
enzyme shows substrate inhibition, pH 7.6, 30°C
20.3
L-glutamate
-
pH 7.6, 37°C, isozyme I from kidney, L-tyrosine as substrate
26.8
L-glutamate
-
pH 7.6, 37°C, isozyme IV from liver, L-tyrosine as substrate
27.4
L-glutamate
-
pH 7.6, 37°C, isozyme III from liver, L-tyrosine as substrate
31.3
L-glutamate
-
pH 7.6, 37°C, isozyme II from liver, L-tyrosine as substrate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activities of different isoenzymes from liver, kidney and heart; effect of glucagon, cyclic nucletides, insulin and hydrocortisone on activity
additional information
-
effect of induction with hydrocortisone on activity
additional information
-
effect of induction with dexamethasone on activity
additional information
-
effect of acute and chronic ethanol administration on synthesis and activity of TAT
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
additional information
-
optimum pH for the isoenzyme TAT-2 is above pH 9.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
30141, 640098, 640099, 640100, 640101, 640102, 640104, 640105, 640107, 640108, 640109, 640112, 640119, 640121, 640122, 640123, 674229, 675591, 702386, 702947
-
-
brenda
4 forms, one of them is probably identical to mitochondrial L-aspartate aminotransferase EC 2.6.1.1
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
fetal hepatocyte primary cultures, synergistic induction of enzyme in presence of glucagon and dexamethasone
brenda
highest transcript level, and also accumulation of rosmarinic acid; highest transcript level, and also accumulation of rosmarinic acid
brenda
additional information
-
-
30141, 640098, 640099, 640100, 640101, 640102, 640103, 640104, 640105, 640107, 640108, 640109, 640112, 640117, 674229, 675591, 702386, 702947
brenda
additional information
transcript level in root is very low, accumulation of rosmarinic acid is 28 times lower in root than in flower; transcript level in root is very low, accumulation of rosmarinic acid is 28 times lower in root than in flower
brenda
additional information
transcript level in root is very low, accumulation of rosmarinic acid is 28 times lower in root than in flower; transcript level in root is very low, accumulation of rosmarinic acid is 28 times lower in root than in flower
brenda
additional information
-
transcript level in root is very low, accumulation of rosmarinic acid is 28 times lower in root than in flower; transcript level in root is very low, accumulation of rosmarinic acid is 28 times lower in root than in flower
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
in vivo analysis by functional complementation shows that the gene is able to complement an Escherichia coli with a background of aminotransferase mutations that confers auxotrophy for L-tyrosine and L-phenylalanine
physiological function
malfunction
-
knock out mutants for the At5g53970 show substantial reduction in TAT activity and a strong increase in tyrosine content. In addition, mutant lines display significantly reduced levels of tocopherols, suggesting a major role of At5g53970 in tocopherol biosynthesis
malfunction
-
virus-induced gene silencing is used to evaluate the contribution of TyrAT to benzylisoquinoline alkaloids metabolism in opium poppy. TyrAT transcript levels were reduced by at least 80% in silenced plants compared with controls and show a moderate reduction in total alkaloid content
physiological function
-
involved in aromatic amino acid metabolism
physiological function
Vitis vinifera x Vitis vinifera
-
involved in aromatic amino acid metabolism
physiological function
Petunia hybrida utilizes a microbial-like phenylpyruvate pathway to produce phenylalanine, and flux through this route is increased when the entry point to the arogenate pathway is limiting. The plant phenylpyruvate pathway utilizes cytosolic tyrosine aminotransferase that links the coordinated catabolism of tyrosine to serve as the amino donor. The enzyme is able to functionally complement the Escherichia coli phenylalanine auxotrophic mutant DL39 which lacks the three aminotransferases, AspC (aspartate aminotransferase), TyrB (L-Tyrosine aminotransferase) and IlvE (branched-chain aminotransferase)
Show AA Sequence and Transmembrane Helices (668 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
110000
50000
90000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
oligomer
tetramer
-
4 * 43000, isoenzyme TAT-1, SDS-PAGE; 4 * 56000, isoenzyme TAT-2, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
liver isoform I is converted into functional lower molecular weight isoenzymes by a lysosomal convertase
additional information
additional information
-
no measurable amount of fucose, mannose, galactose, N-acetylglucose, N-acetylgalactose nor sialic acid
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
through macromolecular crystallography the mTAT crystal structure is determined at 2.9 Å resolution. The crystal structure reveal the interaction between the pyridoxal-5'-phosphate cofactor and the enzyme, as well as the formation of a disulphide bond
-
spontaneous crystallization when enzyme concentration is about 10 mg protein per ml
-
hanging drop vapour diffusion method using 23.6% (w/v) PEG 4000, 0.1 M HEPES, pH 8.0
the crystal structures of the holoenzyme and of the enzyme in complex with the inhibitor 2-aminooxyacetate reveal structural similarity to the beta-phenylalanine aminotransferase from Mesorhizobium sp. strain LUK
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C151Y
-
missense mutation leading to defective folding and likely alteration of the enzymatic activity
L273P
-
missense mutation leading to defective folding and likely alteration of the enzymatic activity
R41A
mutant is inactive when tested with (S)-beta-phenylalanine as amino donor and 2-oxoglutarate as amino acceptor
additional information
-
switch of aspartate aminotransferase to use of tyrosine substrate by introduction of six mutations obtained by rational design and termed HEX plus mutation A293D or mutation I73V
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
additional information
additional information
-
2-oxoglutarate protects against thermal inactivation; pyridoxal 5'-phosphate protects against thermal inactivation
additional information
-
pyridoxal 5'-phosphate protects against thermal inactivation; the apoenzyme is thermally unstable: t1/2 of 2 min at 55°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pyridoxal 5'-phosphate protects against thermal inactivation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM sodium phosphate, pH 6.5, 2 mM EDTA, 1 mM 2-mercaptoethanol, 2.5 mM 2-oxoglutarate
-
-20°C, 50% v/v glycerol, 25 mM phosphate buffer, pH 7.6, 0.1 mM pyridoxal 5'-phosphate, 0.5 mM 2-oxoglutarate, 1 mM DTT, stable for several months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3 enzyme forms isolated using pyridoxamine-affinity column chromatography
-
4 enzyme forms separated by isoelectric focusing and hydroxyapatite chromatography, one of them is probably identical to mitochondrial L-aspartate aminotransferase EC 2.6.1.1
-
high yield procedure using a thermal inactivation of the lysosomal converting factor that generates two additional, lower molecular weight forms
-
nickel Sepharose 6 fast flow chromatography, HiPrep 26/10 desalting column chromatography, and S-75 gel filtration
partial
partial purification of enzyme expressed in Saccharomyces cerevisiae and Escherichia coli using affinity chromatography
-
partial purification of two isoenzymes, using several chromatographic steps
-
partial, using ammonium sulfate precipitation and several chromatographic steps
-
separation of 4 enzyme forms: I, II, III, IV, using hydroxyapatite chromatography
-
three isoenzymes TAT-1, TAT-2 and TAT-3, isolated using anion-exchange chromatography and electrofocusing
-
using Ni-NTA chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression of rat liver enzyme in Saccharomyces cerevisiae and Escherichia coli
-
recombinantly expressed in Escherichia coli as a His-tagged fusion protein
recombinantly expressed in Escherichia coli as a His-tagged fusion protein
recombinantly expressed in Escherichia coli as a His-tagged fusion protein
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in a combined culture of hepatocytes and non-parenchymal liver cells, reproducing intercellular interactions in vitro, cortisol and non-parenchymal cells exhibit an additive effect on TAT activity
-
in starved trout, TyrAT activity in liver and white muscle is about 64 and 267%, respectively, higher than control. After 9 days of refeeding, the control values recover, although, at 6 h of refeeding, hepatic TyrAT activity is higher than that for starvation
-
when rats are maintained on a vitamin B12-deficient diet, the activity of tyrosine aminotransferase in the liver is significantly reduced compared with those in the B12-sufficient control rats
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
tyrosine aminotransferase is not directly associated with resistance to benznidazole, but may act as a general secondary compensatory mechanism or stress response factor. In Trypanosoma cruzi strains resistant o benznidazole, no amplification of the tyrosine aminotransferase gene is observed, and all strain show similar levels of tyrosine aminotransferase mRNA
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gohda, E.; Pitot, H.C.
Purification and characterization of a factor catalyzing the conversion of the multiple forms of tyrosine aminotransferase from rat liver
J. Biol. Chem.
255
7371-7379
1980
Rattus norvegicus
brenda
Miller, J.E.; Litwack, G.
Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase
J. Biol. Chem.
246
3234-3240
1971
Rattus norvegicus
brenda
Hargrove, J.L.; Granner, D.K.
Purification of the native form of tyrosine aminotransferase from rat liver
Anal. Biochem.
104
231-235
1980
Rattus norvegicus
brenda
Lee, K.L.; Roberson, L.E.; Kenney, F.T.
Properties of tyrosine aminotransferase from rat liver
Anal. Biochem.
95
188-193
1979
Rattus norvegicus
brenda
Hargrove, J.L.; Granner, D.K.
Physical properties, limited proteolysis, and acetylation of tyrosine aminotransferase from rat liver
J. Biol. Chem.
256
8012-8017
1981
Rattus norvegicus
brenda
Donner, P.; Wagner, H.; Kröger, H.
Tyrosine aminotransferase from rat liver, a purification in three steps
Biochem. Biophys. Res. Commun.
80
766-772
1978
Rattus norvegicus
brenda
Iwasaki, Y.; Lamar, C.; Danenberg, K.; Pitot, H.C.
Studies on the induction and repression of enzymes in rat liver. Characterization and metabolic regulation of multiple forms of tyrosine aminotransferase
Eur. J. Biochem.
34
347-357
1973
Rattus norvegicus
brenda
Belarbi, A.; Bollack, C.; Befort, N.; Beck, J.P.; Beck, G.
Purification and characterization of rat liver tyrosine aminotransferase
FEBS Lett.
75
221-225
1977
Rattus norvegicus
brenda
Roewekamp, W.; Sekeris, C.E.
Purification and subunit structure of tyrosine aminotransferase from rat liver cytosol
FEBS Lett.
73
225-228
1977
Rattus norvegicus
brenda
Johnson, R.W.; Roberson, L.E.; Kenney, F.T.
Regulation of tyrosine aminotransferase in rat liver. X. Characterization and interconversion of the multiple enzyme forms
J. Biol. Chem.
248
4521-4527
1973
Rattus norvegicus
brenda
Miller, J.V.; Cuatrecasas, P.; Thompson, E.B.
Purification of tyrosine aminotransferase by affinity chromatography
Biochim. Biophys. Acta
276
407-415
1972
Rattus norvegicus
brenda
Jacoby, G.A.; La Du, B.N.
Studies on the specificity of tyrosine-alpha-ketoglutarate transaminase
J. Biol. Chem.
239
419-424
1964
Rattus norvegicus
brenda
Echetebu, C.O.
Some properties of tyrosine aminotransferase from Trichoderma viride
J. Gen. Microbiol.
128
2735-2738
1982
Trichoderma viride
-
brenda
De-Eknamkul, W.; Ellis, B.E.
Purification and characterization of tyrosine aminotransferase activities from Anchusa officinalis cell cultures
Arch. Biochem. Biophys.
257
430-438
1987
Anchusa officinalis
brenda
Dietrich, J.B.; Lorber, B.; Kern, D.
Expression of mammalian tyrosine aminotransferase in Saccharomyces cerevisiae and Escherichia coli. Purification to homogeneity and characterization of the enzyme overproduced in the bacteria
Eur. J. Biochem.
201
399-407
1991
Rattus norvegicus
brenda
Ohisalo, J.J.; Andersson, S.M.; Pispa, J.P.
Partial purification and properties of frog liver tyrosine aminotransferase
Biochem. J.
163
411-417
1977
Rana temporaria
brenda
Rege, A.A.
Purification and characterization of a tyrosine aminotransferase from Crithidia fasciculata
Mol. Biochem. Parasitol.
25
1-9
1987
Crithidia fasciculata
brenda
Echetebu, C.O.; Ifem, F.M.; Echetebu, Z.O.
Hepatic tyrosine aminotransferase from the rainbow lizard Agama agama: purification and some properties
Biochimie
69
223-230
1987
Agama agama
brenda
Belew, K.; Brady, T.
Tyrosine aminotransferase from Drosophila hydei salivary glands: characterization, purification and antibody production
Insect Biochem.
11
239-245
1981
Drosophila hydei
-
brenda
Ohisalo, J.J.; Pispa, J.P.
Heterogeneity of hepatic tyrosine aminotransferase. Separation of the multiple forms from rat and frog liver by isoelectro focussing and hydroxyapatite column chromatography and their partial characterization
Acta Chem. Scand. B
30
491-500
1976
Rana temporaria, Rattus norvegicus
brenda
Montemartini, M.; Santome, J.A.; Cazzulo, J.J.; Nowick, C.
Purification and partial structural and kinetic characterization of tyrosine aminotransferase from epimastigotes of Trypanosoma cruzi
Biochem. J.
292
901-906
1993
Trypanosoma cruzi
brenda
Presch, I.; Birnbacher, R.; Herkner, K.; Lubec, G.
The effect of estradiol and ovariectomy on tyrosine hydroxylase, tyrosine aminotransferase and phenylalanine hydroxylase
Life Sci.
60
479-484
1997
Rattus norvegicus
brenda
Bai, S.C.; Rogers, Q.R.; Wong, D.L.; Sampson, D.A.; Morris, J.G.
Vitamin B-6 deficiency and level of dietary protein affect hepatic tyrosine aminotransferase activity in cats
J. Nutr.
128
1995-2000
1998
Felis catus
brenda
Nimi, S.; Yamaguchi, T.; Hayakawa, T.
Effect of dexamethasone pretreatment on the dexamethasone-dependent induction of tyrosine aminotransferase activity in primary cultured rat hepatocytes
Biol. Pharm. Bull.
21
1009-1012
1998
Rattus norvegicus
brenda
Pickering, C.S.; Watkins, R.H.; Dickson, A.J.
Rat primary hepatocytes and H4 hepatoma cells display differential sensitivity to cyclic AMP at the level of expression of tyrosine aminotransferase
Biochem. Biophys. Res. Commun.
252
764-769
1998
Rattus norvegicus
brenda
Donohue, T.M., Jr.; Drey, M.L.; Zetterman, R.K.
Contrasting effects of acute and chronic ethanol administration on rat liver tyrosine aminotransferase
Alcohol
15
141-146
1998
Rattus norvegicus
brenda
Blankenfeldt, W.; Nowicki, C.; Montemartini-Kalisz, M.; Kalisz, H.M.; Hecht, H.J.
Crystal structure of Trypanosoma cruzi tyrosine aminotransferase: substrate specificity is influenced by cofactor binding mode
Protein Sci.
8
2406-2417
1999
Trypanosoma cruzi
brenda
Ko, T.P.; Wu, S.P.; Yang, W.Z.; Tsai, H.; Yuan, H.S.
Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase
Acta Crystallogr. Sect. D
55
1474-1477
1999
Escherichia coli
brenda
Tabiri, H.Y.; Sato, K.; Takahashi, K.; Toyomizu, M.; Akiba, Y.
Hepatic tyrosine aminotransferase activity is affected by chronic heat stress and dietary tyrosine in broiler chickens
Br. Poult. Sci.
43
629-634
2002
Gallus gallus
brenda
Amin, M.R.; Onodera, R.; Khan, R.I.; Wallace, R.J.; Newbold, C.J.
Purification and properties of glutamate-phenylpyruvate aminotransferase from the ruminal protozoan Entodinium caudatum
Aust. J. Agric. Res.
55
991-997
2004
Entodinium caudatum
-
brenda
Johansson, M.; Johansson, N.; Lund, B.O.
Xenobiotics and the glucocorticoid receptor: additive antagonistic effects on tyrosine aminotransferase activity in rat hepatoma cells
Basic Clin. Pharmacol. Toxicol.
96
309-315
2005
Rattus norvegicus
brenda
Rehman, K.K.; Ayesha, Q.; Khan, A.A.; Ahmed, N.; Habibullah, C.M.
Tyrosine aminotransferase and gamma-glutamyl transferase activity in human fetal hepatocyte primary cultures under proliferative conditions
Cell Biochem. Funct.
22
89-96
2004
Homo sapiens
brenda
Sobrado, V.R.; Montemartini-Kalisz, M.; Kalisz, H.M.; De La Fuente, M.C.; Hecht, H.J.; Nowicki, C.
Involvement of conserved asparagine and arginine residues from the N-terminal region in the catalytic mechanism of rat liver and Trypanosoma cruzi tyrosine aminotransferases
Protein Sci.
12
1039-1050
2003
Rattus norvegicus (P04694), Trypanosoma cruzi (P33447)
brenda
Rothman, S.C.; Voorhies, M.; Kirsch, J.F.
Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase
Protein Sci.
13
763-772
2004
Escherichia coli
brenda
Seetharamappa, J.; Oke, M.; Liu, H.; McMahon, S.A.; Johnson, K.A.; Carter, L.; Dorward, M.; Zawadzki, M.; Overton, I.M.; van Niekirk, C.A.; Graham, S.; Botting, C.H.; Taylor, G.L.; White, M.F.; Barton, G.J.; Coote, P.J.; Naismith, J.H.
Expression, purification, crystallization, data collection and preliminary biochemical characterization of methicillin-resistant Staphylococcus aureus Sar2028, an aspartate/tyrosine/phenylalanine pyridoxal-5-phosphate-dependent aminotransferase
Acta Crystallogr. Sect. F
F63
452-456
2007
Staphylococcus aureus (A0A163U8E7)
brenda
Sivaraman, S.; Kirsch, J.F.
The narrow substrate specificity of human tyrosine aminotransferase--the enzyme deficient in tyrosinemia type II
FEBS J.
273
1920-1929
2006
Homo sapiens
brenda
Dundjerski, J.; Brkljacic, J.; Elakovic, I.; Manitasevic, S.; Matic, G.
Mercury influences rat liver tyrosine aminotransferase activity and induction by dexamethasone
J. Appl. Toxicol.
26
187-190
2006
Rattus norvegicus
brenda
Minami-Hori, M.; Ishida-Yamamoto, A.; Katoh, N.; Takahashi, H.; Iizuka, H.
Richner-Hanhart syndrome: Report of a case with a novel mutation of tyrosine aminotransferase
J. Dermatol. Sci.
41
82-84
2006
Homo sapiens
brenda
Hazra, A.; Pyszczynski, N.; Dubois, D.C.; Almon, R.R.; Jusko, W.J.
Modeling receptor/gene-mediated effects of corticosteroids on hepatic tyrosine aminotransferase dynamics in rats: dual regulation by endogenous and exogenous corticosteroids
J. Pharmacokinet. Pharmacodyn.
34
643-667
2007
Rattus norvegicus
brenda
Hollaender-Czytko, H.; Grabowski, J.; Sandorf, I.; Weckermann, K.; Weiler, E.W.
Tocopherol content and activities of tyrosine aminotransferase and cystine lyase in Arabidopsis under stress conditions
J. Plant Physiol.
162
767-770
2005
Arabidopsis thaliana
brenda
Charfeddine, C.; Monastiri, K.; Mokni, M.; Laadjimi, A.; Kaabachi, N.; Perin, O.; Nilges, M.; Kassar, S.; Keirallah, M.; Guediche, M.N.; Kamoun, M.R.; Tebib, N.; Ben Dridi, M.F.; Boubaker, S.; Ben Osman, A.; Abdelhak, S.
Clinical and mutational investigations of tyrosinemia type II in Northern Tunisia: Identification and structural characterization of two novel TAT mutations
Mol. Genet. Metab.
88
184-191
2006
Homo sapiens
brenda
Rego, J.V.; Murta, S.M.; Nirde, P.; Nogueira, F.B.; de Andrade, H.M.; Romanha, A.J.
Trypanosoma cruzi: characterisation of the gene encoding tyrosine aminotransferase in benznidazole-resistant and susceptible populations
Exp. Parasitol.
118
111-117
2008
Trypanosoma cruzi (Q4E4E7), Trypanosoma cruzi
brenda
Panin, L.E.; Usynin, I.F.
Role of glucocorticoids and resident liver macrophages in induction of tyrosine aminotransferase
Biochemistry
73
305-309
2008
Rattus norvegicus
brenda
Ebara, S.; Nakao, M.; Tomoda, M.; Yamaji, R.; Watanabe, F.; Inui, H.; Nakano, Y.
Vitamin B12 deficiency results in the abnormal regulation of serine dehydratase and tyrosine aminotransferase activities correlated with impairment of the adenylyl cyclase system in rat liver
Br. J. Nutr.
99
503-510
2008
Rattus norvegicus
brenda
Peragon, J.; Barroso, J.; De la Higuera, M.; Lupianez, J.
Serine dehydratase and tyrosine aminotransferase activities increased by long-term starvation and recovery by refeeding in rainbow trout (Oncorhynchus mykiss)
J. Exp. Zool. Part A Ecol. Genet. Physiol.
309
25-34
2008
Oncorhynchus mykiss
brenda
Marciano, D.; Maugeri, D.A.; Cazzulo, J.J.; Nowicki, C.
Functional characterization of stage-specific aminotransferases from trypanosomatids
Mol. Biochem. Parasitol.
166
172-182
2009
Leishmania major
brenda
Battilana, J.; Costantini, L.; Emanuelli, F.; Sevini, F.; Segala, C.; Moser, S.; Velasco, R.; Versini, G.; Stella Grando, M.
The 1-deoxy-D: -xylulose 5-phosphate synthase gene co-localizes with a major QTL affecting monoterpene content in grapevine
Theor. Appl. Genet.
118
653-669
2009
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
brenda
Crismaru, C.G.; Wybenga, G.G.; Szymanski, W.; Wijma, H.J.; Wu, B.; Bartsch, S.; de Wildeman, S.; Poelarends, G.J.; Feringa, B.L.; Dijkstra, B.W.; Janssen, D.B.
Biochemical properties and crystal structure of a beta-phenylalanine aminotransferase from Variovorax paradoxus
Appl. Environ. Microbiol.
79
185-195
2013
Variovorax paradoxus (H8WR05)
brenda
Prabhu, P.R.; Hudson, A.O.
Identification and partial characterization of an L-tyrosine aminotransferase (TAT) from Arabidopsis thaliana
Biochem. Res. Int.
2010
549572
2010
Arabidopsis thaliana, Arabidopsis thaliana (Q9LVY1)
brenda
Grossmann, K.; Hutzler, J.; Tresch, S.; Christiansen, N.; Looser, R.; Ehrhardt, T.
On the mode of action of the herbicides cinmethylin and 5-benzyloxymethyl-1, 2-isoxazolines: putative inhibitors of plant tyrosine aminotransferase
Pest Manag. Sci.
68
482-492
2012
Arabidopsis thaliana
brenda
Riewe, D.; Koohi, M.; Lisec, J.; Pfeiffer, M.; Lippmann, R.; Schmeichel, J.; Willmitzer, L.; Altmann, T.
A tyrosine aminotransferase involved in tocopherol synthesis in Arabidopsis
Plant J.
71
850-859
2012
Arabidopsis thaliana
brenda
Lee, E.J.; Facchini, P.J.
Tyrosine aminotransferase contributes to benzylisoquinoline alkaloid biosynthesis in opium poppy
Plant Physiol.
157
1067-1078
2011
Papaver somniferum
brenda
Mehere, P.; Han, Q.; Lemkul, J.A.; Vavricka, C.J.; Robinson, H.; Bevan, D.R.; Li, J.
Tyrosine aminotransferase: biochemical and structural properties and molecular dynamics simulations
Protein Cell
1
1023-1032
2010
Mus musculus
brenda
Yoo, H.; Widhalm, J.; Qian, Y.; Maeda, H.; Cooper, B.; Jannasch, A.; Gonda, I.; Lewinsohn, E.; Rhodes, D.; Dudareva, N.
An alternative pathway contributes to phenylalanine biosynthesis in plants via a cytosolic tyrosine:phenylpyruvate aminotransferase
Nat. Commun.
4
2833
2013
Petunia x hybrida (V5M241)
brenda
Kim, Y.B.; Uddina, M.R.; Kim, Y.; Park, C.G.; Park, S.U.
Molecular cloning and characterization of tyrosine aminotransferase and hydroxyphenylpyruvate reductase, and rosmarinic acid accumulation in Scutellaria baicalensis
Nat. Prod. Commun.
9
1311-1314
2014
Scutellaria baicalensis (A0A0A7DPK0), Scutellaria baicalensis (A0A0A7DQ59), Scutellaria baicalensis
brenda
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