Information on EC 2.6.1.5 - tyrosine transaminase

for references in articles please use BRENDA:EC2.6.1.5
Word Map on EC 2.6.1.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


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

top print hide
EC NUMBER
COMMENTARY hide
2.6.1.5
-
top print hide
RECOMMENDED NAME
GeneOntology No.
tyrosine transaminase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(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)
-
-
rosmarinic acid biosynthesis I
-
-
methionine metabolism
-
-
tyrosine metabolism
-
-
Ubiquinone and other terpenoid-quinone biosynthesis
-
-
Cysteine and methionine metabolism
-
-
Tyrosine metabolism
-
-
Phenylalanine metabolism
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
Novobiocin biosynthesis
-
-
Isoquinoline alkaloid biosynthesis
-
-
Tropane, piperidine and pyridine alkaloid biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
top print hide
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].
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
9014-55-5
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
rainbow lizard
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
chicken
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
Q6GFC0
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis vinifera
-
-
-
Manually annotated by BRENDA team
top print hide
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2-aminophenyl)alanine + 2-oxoglutarate
3-(4-aminophenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
10% of the activity that with L-tyrosine
-
?
(3-fluorophenyl)alanine + 2-oxoglutarate
3-(3-fluorophenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
4% of the activity that with L-tyrosine
-
?
(4-chlorophenyl)alanine + 2-oxoglutarate
3-(3-chlorophenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
17% of the activity with L-tyrosine
-
?
(4-fluorophenyl)alanine + 2-oxoglutarate
3-(4-fluorophenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
7.9% of the activity that with L-tyrosine
-
?
(R)-3-amino-5-methyl-hexanoic acid + 2-oxoglutarate
?
show the reaction diagram
relative activity: 48%
-
-
?
(S)-beta-phenylalanine + 2-oxoglutarate
3-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
relative activity: 100%
-
-
?
(S)-beta-phenylalanine + pyruvate
3-oxo-3-phenylpropionic acid + L-alanine
show the reaction diagram
the activity of VpAT with pyruvate is 85% of that with alpha-ketoglutarate as the amino acceptor
-
-
?
2-oxoglutarate + L-phenylalanine
L-glutamate + phenylpyruvate
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenylalanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
L-tyrosine + 2-oxoglutarate
show the reaction diagram
-
-
-
r
3-aminotyrosine + 2-oxoglutarate
3-(3-amino-4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
16% of the activity than with L-tyrosine
-
?
3-iodotyrosine + 2-oxoglutarate
3-(4-hydroxy-3-iodophenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
3-methoxytyrosine + 2-oxoglutarate
3-(3-methoxy-4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
22% of the activity with L-tyrosine
-
?
4-hydroxyphenylpyruvate + L-aspartate
L-tyrosine + oxaloacetate
show the reaction diagram
-
35% of the activity with L-glutamate
-
r
4-hydroxyphenylpyruvate + L-phenylalanine
L-glutamate + phenylpyruvate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoisocaproate
pyruvate + 2-aminoisocaproate
show the reaction diagram
-
-
-
?
L-asparagine + 2-oxoglutarate
2-oxosuccinamate + L-glutamate
show the reaction diagram
-
15% of the activity with L-tyrosine
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
L-cysteine + 2-oxoglutarate
3-mercapto-2-oxopropanoate + L-glutamate
show the reaction diagram
-
higher activity than with L-tyrosine
-
?
L-ethionine + 2-oxoglutarate
4-ethylsulfanyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
17% of the activity than with L-tyrosine
-
?
L-glutamate + 4-hydroxyphenylpyruvate
2-oxoglutarate + L-tyrosine
show the reaction diagram
L-glutamate + 4-hydroxyphenylpyruvate
L-tyrosine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
L-glutamate + phenylpyruvate
2-oxoglutarate + L-phenylalanine
show the reaction diagram
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
show the reaction diagram
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropanoate + L-glutamate
show the reaction diagram
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
L-tryptophan + 2-oxoglutarate
3-(1H-indol-3-yl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tryptophan + oxaloacetate
3-(1H-indol-3-yl)-2-oxopropanoate + L-glycine
show the reaction diagram
-
-
-
-
?
L-tryptophan + pyruvate
3-(1H-indol-3-yl)-2-oxopropanoate + L-alanine
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
L-tyrosine + 2-oxohexanoate
3-(4-hydroxyphenyl)-2-oxopropanoate + (2S)-2-aminohexanoate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxopentanoate
3-(4-hydroxyphenyl)-2-oxopropanoate + (2S)-2-aminopentanoate
show the reaction diagram
relative activity compared to 2-oxoglutarate: 3%
-
-
?
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
show the reaction diagram
L-tyrosine + oxaloacetate
?
show the reaction diagram
relative activity compared to 2-oxoglutarate: 75%
-
-
?
L-tyrosine + phenylpyruvate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
L-tyrosine + phenylpyruvate
4-hydroxyphenylpyruvate + L-phenylalanine
show the reaction diagram
-
-
-
r
L-tyrosine + prephenate
?
show the reaction diagram
relative activity compared to 2-oxoglutarate: 23%
-
-
?
L-tyrosine + pyruvate
4-hydroxyphenylpyruvate + L-alanine
show the reaction diagram
-
-
-
?
L-tyrosine + pyruvate
?
show the reaction diagram
relative activity compared to 2-oxoglutarate: 40%
-
-
?
rac-2-fluoro-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 15%
-
-
?
rac-2-methyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 5%
-
-
?
rac-3-bromo-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 53%
-
-
?
rac-3-chloro-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 56%
-
-
?
rac-3-fluoro-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 48%
-
-
?
rac-3-methyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 54%
-
-
?
rac-4-bromo-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 62%
-
-
?
rac-4-ethyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 134%
-
-
?
rac-4-fluoro-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 87%
-
-
?
rac-4-iso-propyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 61%
-
-
?
rac-4-methyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 100%
-
-
?
rac-4-nitro-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 32%
-
-
?
rac-4-nitro-hydroxy-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 61%
-
-
?
rac-4-propyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 126%
-
-
?
rac-4-trifluoromethyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 73%
-
-
?
rac-beta-leucine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 38%
-
-
?
rac-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
relative activity: 100%
-
-
?
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
additional information
?
-
top print hide
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-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate
-
can replace pyridoxal 5'-phosphate
top print hide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Hg2+
-
a dose of 1-3 mg/kg increases the basal activity of the enzyme and decreases its induction by dexamethasone
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4-hydroxyphenyl)acetic acid
-
74% inhibition with tyrosine at 3 mM and (4-hydroxyphenyl)acetic acid at 12 mM
2-aminooxyacetate
-
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
2-oxoglutarate
3,4-dihydroxyphenylalanine
-
-
3,4-Dihydroxyphenyllactate
-
strong inhibition of all the three TAT isoenzymes
3-(3,4-Dihydroxyphenyl)-2-methylalanine
-
-
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
3-methoxydopamine
-
-
3-Methoxytyrosine
-
-
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
Ag2+
-
-
AgNO3
-
10 mM, complete inhibition
alpha-Methyl-L-aspartate
-
with L-tyrosine and 2-oxoglutarate or oxaloacetate as substrates
alpha-Methyltyrosine
-
-
Aminooxyacetate
beta-Methyl-L-aspartate
-
with L-tyrosine and 2-oxoglutarate or oxaloacetate as substrates
beta-phenylalanine
enzyme shows substrate inhibition
Ca2+
-
-
Canaline
cinmethylin
-
0.5 mM: 96% inhibition of enzyme activity, 0.25 mM: 20% inhibition of enzyme activity
CuSO4
-
10 mM, complete inhibition
D-Aspartate
-
weak inhibition
D-tyrosine
-
9% inhibition with tyrosine at 3 mM and D-tyrosine at 12 mM
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
dopamine
-
100% inhibition with tyrosine at 3 mM and dopamine at 12 mM
EDTA
-
1 mM, 21% residual activity
Hg2+
-
-
homogentisate
-
half-maximal inhibition with 15 micromolar
homovanillic acid
-
-
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
kynuric acid
-
10 mM, complete inhibition
L-aspartate
-
with L-tyrosine and 2-oxoglutarate or oxaloacetate as substrates
L-glutamate
methiozolin
-
0.5 mM: 91% inhibition of enzyme activity, 0.25 mM: 57% inhibition of enzyme activity
Mn2+
-
-
norepinephrine
-
competitive inhibition
normetanephrine
-
-
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
phenylhydrazine
-
1 mM, complete inhibition
rosmarinic acid
-
isoenzymes TAT-2 and TAT-3
serotonin
-
37% inhibition with tyrosine at 3 mM and serotonin at 12 mM
SnCl2
-
10 mM, complete inhibition
sodium dodecylsulfate
-
1 mM, complete inhibition
tolylfluanid
-
significant reduction of dexamethasone-induced activity, 50% inhibition at 0.0014 mM
tyramine
-
13% inhibition with tyrosine at 3 mM and tyramine at 12 mM
vanillylmandelic acid
-
51% inhibition with tyrosine at 3 mM and vanillylmandelic acid at 3 mM
Zn2+
-
-
top print hide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adrenaline
-
activation is independent of the concentration of tyrosine, maximal activation achieved with 7-10 micromolar of adrenaline
dexamethasone
dopamine
-
slight activation
metanephrine
-
slight activation
noradrenaline
-
slight activation
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
(S)-beta-phenylalanine
pH 7.6, 30°C
0.13
2-oxo-3-phenylpropanoate
pH 8.2, 30°C
0.19 - 3300
2-oxoglutarate
7.3
2-Oxohexanoate
-
pH 7.0, 38°C
0.3 - 20.4
2-oxoisocaproate
26
3,4-dihydroxyphenylalanine
-
pH 7.9, 37°C
0.22
3-(4-hydroxyphenyl)-2-oxopropanoate
pH 8.2, 30°C
0.7 - 7.9
4-hydroxyphenylpyruvate
0.9 - 1.2
L-alanine
1.4 - 11.1
L-glutamate
0.84 - 13.8
L-phenylalanine
7.83
L-tryptophan
-
pH 8.5, 30°C
0.19 - 870
L-tyrosine
16 - 56.13
oxaloacetate
1.2 - 580
p-hydroxyphenylpyruvate
17.9 - 80
phenylalanine
0.9 - 2.6
phenylpyruvate
0.5 - 2.45
pyruvate
21.4 - 60
tryptophan
additional information
additional information
-
top print hide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.8
(S)-beta-phenylalanine
pH 7.6, 30°C
0.22 - 566
2-oxoglutarate
1.83
2-Oxohexanoate
-
pH 7.0, 38°C
0.4 - 34
2-oxoisocaproate
0.7 - 15.83
4-hydroxyphenylpyruvate
0.35 - 23.5
L-alanine
0.44 - 210
L-glutamate
0.08 - 15.33
L-phenylalanine
0.36
L-tryptophan
-
pH 8.5, 30°C
0.24 - 576
L-tyrosine
0.37
oxaloacetate
-
pH 8.5, 30°C
1.2 - 165
p-hydroxyphenylpyruvate
1.19 - 2.66
phenylpyruvate
0.34 - 47.4
pyruvate
top print hide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.51 - 14.16
2-oxoglutarate
0.33
2-Oxohexanoate
-
pH 7.0, 38°C
0.09 - 22.66
4-hydroxyphenylpyruvate
0.04 - 2
L-glutamate
0.01 - 1.33
L-phenylalanine
0.13 - 10.66
L-tyrosine
0.01
oxaloacetate
-
pH 8.5, 30°C
0.46 - 3
phenylpyruvate
0.14
pyruvate
-
pH 8.5, 30°C
top print hide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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 - 31.3
L-glutamate
additional information
additional information
-
inhibition due to L-glutamate
-
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
203
-
isoenzyme I
416
-
enzyme expressed in Escherichia coli
1200
-
from rats stimulated with corticosterone and dexamethasone
additional information
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
7.7
-
recombinant enzyme expressed in Escherichia coli
9
-
L-tyrosine as substrate, isoenzyme TAT-1
additional information
-
optimum pH for the isoenzyme TAT-2 is above pH 9.6
top print hide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11.2
enzyme shows high activity over a broad pH range
8.8 - 9.4
-
L-tyrosine as substrate, isoenzyme TAT-3
additional information
-
-
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
-
assay at
40
-
assay at
top print hide
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 70
-
highest activity
55
-
decrease in activity above
top print hide
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.25
Q6GFC0
2D-PAGE
top print hide
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
fetal hepatocyte primary cultures, synergistic induction of enzyme in presence of glucagon and dexamethasone
Manually annotated by BRENDA team
highest transcript level, and also accumulation of rosmarinic acid; highest transcript level, and also accumulation of rosmarinic acid
Manually annotated by BRENDA team
-
Reuber hepatoma cell line
Manually annotated by BRENDA team
-
transcripts highly detected
Manually annotated by BRENDA team
-
transcripts highly detected
Manually annotated by BRENDA team
additional information
top print hide
top print hide
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
x * 42000, SDS-PAGE
43000
-
4 * 43000, isoenzyme TAT-1, SDS-PAGE
44000
-
2 * 44000, isoenzymes TAT-I and TAT-II, SDS-PAGE
45000
-
2 * 45000, SDS-PAGE
46420
calculated from cDNA
48000
-
1 * 50000 + 1 * 48000
48170
Q6GFC0
X-ray crystallography
49600
-
calculated from amino acid sequence
52000
-
x * 52000, SDS-PAGE
53000
-
2 * 53000, SDS-PAGE
56000
-
4 * 56000, isoenzyme TAT-2, SDS-PAGE
65000
-
x * 65000, SDS-PAGE
85000
-
gel filtration, isoforms I and II
91000
-
gel filtration
100000
104500
-
ultracentrifugation
105000
-
glycerol gradient centrifugation
107000
-
gel filtration, different isoenzymes
110000
110500
-
sucrose density gradient sedimentation
114000
-
sedimentation analysis
130000
-
-
150000
-
recombinant expressed in Escherichia coli, native gradient PAGE
160000
-
recombinant expressed in Escherichia coli, gel filtration
180000
-
isoenzyme TAT-1, gel filtration
220000
-
isoenzymes TAT-2 and TAT-3, gel filtration
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
-
1 * 50000 + 1 * 48000
monomer
-
1 * ?, SDS-PAGE
oligomer
tetramer
-
4 * 43000, isoenzyme TAT-1, SDS-PAGE; 4 * 56000, isoenzyme TAT-2, SDS-PAGE
top print hide
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
liver isoform I is converted into functional lower molecular weight isoenzymes by a lysosomal convertase
additional information
top print hide
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
low resolution structure of the enzyme bound to pyridoxal 5'-phosphate
-
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
Q6GFC0
structure determined at 2.5 A resolution
-
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
top print hide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
15 min, 50% loss of activity, isoenzyme TAT-3
55
-
15 min, 50% loss of activity, isoenzyme TAT-2
60
-
stable below
additional information
top print hide
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate protects against thermal inactivation
-
pyridoxal 5'-phosphate protects against thermal inactivation
sensitive to SH inactivation
-
top print hide
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
-
top print hide
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
-
isoenzymes TAT-I and TAT-II
-
native and one of the modified forms
-
Ni-NTA column chromatography
-
nickel Sepharose 6 fast flow chromatography, HiPrep 26/10 desalting column chromatography, and S-75 gel filtration
Q6GFC0
NTA-resin column chromatography
-
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
-
partial, using chromatography on DEAE-cellulose and gel filtration
-
partial, using gel filtration
-
partial, using pyridoxamine-affinity column cheomatography
-
partial, using Sephadex chromatography and isoelectrofocusing
-
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 affinity, Source-Q and gel-filtration chromatography
-
using Ni-NTA chromatography
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21-CodonPlus (DE3)RIL cells
-
expression of rat liver enzyme in Saccharomyces cerevisiae and Escherichia coli
-
recombinantly expressed in Escherichia coli as a His-tagged fusion protein
top print hide
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
-
top print hide
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C151Y
-
missense mutation leading to defective folding and likely alteration of the enzymatic activity
I249A
-
reduced catalytic activity
L273P
-
missense mutation leading to defective folding and likely alteration of the enzymatic activity
N54S
reduced enzymic activity
R315K
retains enzymic activity
R417Q
no enzymic activity
R57A
no enzymic activity
R57Q
no enzymic activity
N17S
increase in Km-values, substantial decrease in kcat-values
R20A
increase in Km-values, substantial decrease in kcat-values
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
top print hide
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
top
Show AA Sequence (143 entries)
Please use the Sequence Search for a specific query.
top
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 2.6.1.5)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)