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L-glutamate + 4-hydroxyphenylpyruvate
2-oxoglutarate + L-tyrosine
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
?
(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
-
?
3,4-dihydroxyphenylalanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
3-aminotyrosine + 2-oxoglutarate
3-(3-amino-4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
-
16% of the activity than with L-tyrosine
-
?
3-iodotyrosine + 2-oxoglutarate
3-(4-hydroxy-3-iodophenyl)-2-oxopropanoate + L-glutamate
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
L-asparagine + 2-oxoglutarate
2-oxosuccinamate + L-glutamate
-
15% of the activity with L-tyrosine
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
higher activity than 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-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
20% of the activity than with L-tyrosine
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
-
-
-
r
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
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-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-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
-
maximal activity with L-tyrosine
-
?
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
-
?
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(4-hydroxyphenyl)acetic acid
-
74% inhibition with tyrosine at 3 mM and (4-hydroxyphenyl)acetic acid at 12 mM
3,4-dihydroxyphenylalanine
-
-
3-(3,4-Dihydroxyphenyl)-2-methylalanine
-
-
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
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
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
norepinephrine
-
competitive inhibition
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
serotonin
-
37% inhibition with tyrosine at 3 mM and serotonin at 12 mM
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
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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.; Krger, 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
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.; 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
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
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
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
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
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
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
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
Nandi, S.S.; Zheng, H.; Sharma, N.M.; Shahshahan, H.R.; Patel, K.P.; Mishra, P.K.
Lack of miR-133a decreases contractility of diabetic hearts a role for novel cross talk between tyrosine aminotransferase and tyrosine hydroxylase
Diabetes
65
3075-3090
2016
Rattus norvegicus (P04694), Mus musculus (Q8QZR1)
brenda