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Information on EC 2.6.1.5 - tyrosine transaminase and Organism(s) Rattus norvegicus and UniProt Accession P04694

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.5 tyrosine transaminase
IUBMB 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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Rattus norvegicus
UNIPROT: P04694
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
tyrosine aminotransferase, tyrosine transaminase, tatase, tyrat, tyrosine-alpha-ketoglutarate transaminase, l-tyrosine:2-oxoglutarate aminotransferase, phenylalanine aminotransferase, at5g53970, phenylalanine transaminase, l-tyrosine aminotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tyrosine aminotransferase
-
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
-
-
-
-
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9014-55-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamate + 4-hydroxyphenylpyruvate
2-oxoglutarate + L-tyrosine
show the reaction diagram
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
?
(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
-
?
3,4-dihydroxyphenylalanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
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
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
-
higher activity than with L-tyrosine
-
?
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-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
20% of the activity than with L-tyrosine
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
show the reaction diagram
-
-
-
r
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate
-
can replace pyridoxal 5'-phosphate
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
INHIBITOR
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
3,4-dihydroxyphenylalanine
-
-
3-(3,4-Dihydroxyphenyl)-2-methylalanine
-
-
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
alpha-Methyl-L-aspartate
-
with L-tyrosine and 2-oxoglutarate or oxaloacetate as substrates
alpha-Methyltyrosine
-
-
beta-Methyl-L-aspartate
-
with L-tyrosine and 2-oxoglutarate or oxaloacetate as substrates
Canaline
-
-
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
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
L-aspartate
-
with L-tyrosine and 2-oxoglutarate or oxaloacetate as substrates
L-glutamate
-
-
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
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dexamethasone
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35 - 3.5
2-oxoglutarate
1.9 - 8.8
L-glutamate
2.1 - 5.3
L-tyrosine
1.2 - 1.3
p-hydroxyphenylpyruvate
0.7 - 1.2
2-oxoglutarate
26
3,4-dihydroxyphenylalanine
-
pH 7.9, 37°C
1.4 - 15
L-tyrosine
80
phenylalanine
-
pH 7.9, 37°C
30 - 60
tryptophan
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
116 - 566
2-oxoglutarate
6.6 - 210
L-glutamate
132 - 576
L-tyrosine
5.9 - 165
p-hydroxyphenylpyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20.3 - 31.3
L-glutamate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1200
-
from rats stimulated with corticosterone and dexamethasone
416
-
enzyme expressed in Escherichia coli
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
-
recombinant enzyme expressed in Escherichia coli
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Swissprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme inhibits tyrosine hydroxylase in neuronal cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ATTY_RAT
454
0
50635
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
gel filtration
104500
-
ultracentrifugation
105000
-
glycerol gradient centrifugation
107000
-
gel filtration, different isoenzymes
110000
-
recombinant expressed in Escherichia coli, ultracentrifugation
110500
-
sucrose density gradient sedimentation
114000
-
sedimentation analysis
150000
-
recombinant expressed in Escherichia coli, native gradient PAGE
160000
-
recombinant expressed in Escherichia coli, gel filtration
44000
-
2 * 44000, isoenzymes TAT-I and TAT-II, SDS-PAGE
50000
52000
-
x * 52000, SDS-PAGE
53000
-
2 * 53000, SDS-PAGE
90000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 50000, SDS-PAGE
dimer
oligomer
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
-
no measurable amount of fucose, mannose, galactose, N-acetylglucose, N-acetylgalactose nor sialic acid
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
spontaneous crystallization when enzyme concentration is about 10 mg protein per ml
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N54S
reduced enzymic activity
R315K
retains enzymic activity
R417Q
no enzymic activity
R57A
no enzymic activity
R57Q
no enzymic activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pyridoxal 5'-phosphate protects against thermal inactivation
-
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
-
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
-
partial purification of enzyme expressed in Saccharomyces cerevisiae and Escherichia coli using affinity chromatography
-
partial, using pyridoxamine-affinity column cheomatography
-
partial, using Sephadex chromatography and isoelectrofocusing
-
separation of 4 enzyme forms: I, II, III, IV, using hydroxyapatite chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of rat liver enzyme in Saccharomyces cerevisiae and Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
miR-133a mimic treatment improves the contractility of the diabetic rat's heart concomitant with downregulation of the enzyme
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
-
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
-
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
Manually annotated by BRENDA team
Miller, J.E.; Litwack, G.
Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase
J. Biol. Chem.
246
3234-3240
1971
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Lee, K.L.; Roberson, L.E.; Kenney, F.T.
Properties of tyrosine aminotransferase from rat liver
Anal. Biochem.
95
188-193
1979
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Roewekamp, W.; Sekeris, C.E.
Purification and subunit structure of tyrosine aminotransferase from rat liver cytosol
FEBS Lett.
73
225-228
1977
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Miller, J.V.; Cuatrecasas, P.; Thompson, E.B.
Purification of tyrosine aminotransferase by affinity chromatography
Biochim. Biophys. Acta
276
407-415
1972
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team