Information on EC 2.6.1.5 - tyrosine transaminase

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

EC NUMBER
COMMENTARY
2.6.1.5
-
RECOMMENDED NAME
GeneOntology No.
tyrosine transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
(S)-reticuline biosynthesis I
-
4-hydroxyphenylpyruvate biosynthesis
-
Biosynthesis of secondary metabolites
-
Cysteine and methionine metabolism
-
Isoquinoline alkaloid biosynthesis
-
Metabolic pathways
-
Novobiocin biosynthesis
-
Phenylalanine metabolism
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
rosmarinic acid biosynthesis I
-
Tropane, piperidine and pyridine alkaloid biosynthesis
-
tyrosine biosynthesis I
-
tyrosine degradation I
-
tyrosine degradation II
-
tyrosine degradation III
-
Tyrosine metabolism
-
Ubiquinone and other terpenoid-quinone biosynthesis
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aminotransferase, tyrosine
-
-
-
-
At5g36160
Q9LVY1
gene name
At5g53970
-
gene name
beta-phenylalanine aminotransferase
H8WR05
-
glutamic phenylpyruvic aminotransferase
-
-
-
-
glutamic-hydroxyphenylpyruvic transaminase
-
-
-
-
L-phenylalanine 2-oxoglutarate aminotransferase
-
-
-
-
L-tyrosine aminotransferase
-
-
-
-
mTAT
-
-
phenylalanine aminotransferase
-
-
-
-
phenylalanine transaminase
-
-
-
-
phenylalanine-alpha-ketoglutarate transaminase
-
-
-
-
phenylpyruvate transaminase
-
-
-
-
phenylpyruvic acid transaminase
-
-
-
-
Sar2028
Q6GFC0
-
TAT
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
-
-
TATase
-
-
TATc
-
-
tyrosine aminotransferase
-
-
-
-
tyrosine aminotransferase
-
-
tyrosine aminotransferase
-
-
tyrosine aminotransferase
-
-
tyrosine aminotransferase
-
-
tyrosine aminotransferase
-
-
tyrosine aminotransferase
-
-
tyrosine aminotransferase
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
-
-
tyrosine-2-ketoglutarate aminotransferase
-
-
-
-
tyrosine-2-oxoglutarate aminotransferase
-
-
-
-
tyrosine-alpha-ketoglutarate aminotransferase
-
-
-
-
tyrosine-alpha-ketoglutarate transaminase
-
-
-
-
L-tyrosine-2-oxoglutarate aminotransferase
-
-
-
-
additional information
-
the mitochondrial enzyme may be identical with EC 2.6.1.1 and with EC 2.6.1.57
CAS REGISTRY NUMBER
COMMENTARY
9014-55-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
rainbow lizard
-
-
Manually annotated by BRENDA team
chicken
-
-
Manually annotated by BRENDA team
enzyme is not suppressed during cell proliferation
-
-
Manually annotated by BRENDA team
4 enzyme forms from kidney, heart and brain
-
-
Manually annotated by BRENDA team
4 forms, one of them is probably identical to mitochondrial L-aspartate aminotransferase EC 2.6.1.1
-
-
Manually annotated by BRENDA team
induction of enzyme by dexamethasone
-
-
Manually annotated by BRENDA team
epimastigote
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis riparia
-
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis vinifera
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
metabolism
-, Q9LVY1
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
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
-
involved in aromatic amino acid metabolism
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
H8WR05
relative activity: 48%
-
-
?
(S)-beta-phenylalanine + 2-oxoglutarate
3-oxo-3-phenylpropionic acid + L-glutamate
show the reaction diagram
H8WR05
relative activity: 100%
-
-
?
(S)-beta-phenylalanine + pyruvate
3-oxo-3-phenylpropionic acid + L-alanine
show the reaction diagram
H8WR05
the activity of VpAT with pyruvate is 85% of that with alpha-ketoglutarate as the amino acceptor
-
-
?
3,4-dihydroxyphenylalanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenylalanine + 2-oxoglutarate
3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
85% of the activity than with L-tyrosine
-
?
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
L-tyrosine + 2-oxoglutarate
show the reaction diagram
-, Q9LVY1
-
-
-
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
-
as effective as L-tyrosine
-
?
3-iodotyrosine + 2-oxoglutarate
3-(4-hydroxy-3-iodophenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
84% of the activity than with L-tyrosine
-
?
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-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
P33447
-
-
-
?
L-alanine + 2-oxoisocaproate
pyruvate + 2-aminoisocaproate
show the reaction diagram
P33447
-
-
-
?
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
-
isoenzymes TAT-2 and TAT-3, best substrate for isoenzyme TAT-3
-
?
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-glutamate + 4-hydroxyphenylpyruvate
L-tyrosine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
L-glutamate + p-hydroxyphenylpyruvate
2-oxoglutarate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
L-glutamate + p-hydroxyphenylpyruvate
2-oxoglutarate + L-phenylalanine
show the reaction diagram
P04694
-
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
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-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
no activity
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
lower activity than with L-tyrosine
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
higher rate than with L-tyrosine
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropanoate + L-glutamate
show the reaction diagram
-, Q9LVY1
-
-
-
r
L-tryptophane + 2-oxoglutarate
3-(1H-indol-3-yl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tryptophane + oxaloacetate
3-(1H-indol-3-yl)-2-oxopropanoate + L-glycine
show the reaction diagram
-
-
-
-
?
L-tryptophane + 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
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-, Q9LVY1
best substrate
-
-
r
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
r
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
P04694
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
Q6GFC0
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
maximal activity with L-tyrosine
-
-
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
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
show the reaction diagram
-
highly specific for: L-tyrosine
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
highly specific for: L-tyrosine
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
specific for 2-oxoglutarate as the amino group acceptor
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
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, first step in tyrosine pathway leading to the formation of rosmarinic acid (alpha-O-caffeoyl-3,4-dihydroxyphenyllactic acid)
-
?
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
-, Q9LVY1
relative activity compared to 2-oxoglutarate: 3%
-
-
?
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
show the reaction diagram
-
-
-
r
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
show the reaction diagram
-
-
-
?
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
show the reaction diagram
-
-
-
?
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
show the reaction diagram
-
no activity
-
?
L-tyrosine + oxaloacetate
4-hydroxyphenylpyruvate + L-aspartate
show the reaction diagram
-
no activity
-
?
L-tyrosine + oxaloacetate
?
show the reaction diagram
-, Q9LVY1
relative activity compared to 2-oxoglutarate: 75%
-
-
?
L-tyrosine + phenylpyruvate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
L-tyrosine + prephenate
?
show the reaction diagram
-, Q9LVY1
relative activity compared to 2-oxoglutarate: 23%
-
-
?
L-tyrosine + pyruvate
4-hydroxyphenylpyruvate + L-alanine
show the reaction diagram
P33447
-
-
-
?
rac-2-fluoro-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 15%
-
-
?
rac-2-methyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 5%
-
-
?
rac-3-bromo-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 53%
-
-
?
rac-3-chloro-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 56%
-
-
?
rac-3-fluoro-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 48%
-
-
?
rac-3-methyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 54%
-
-
?
rac-4-bromo-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 62%
-
-
?
rac-4-ethyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 134%
-
-
?
rac-4-fluoro-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 87%
-
-
?
rac-4-iso-propyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 61%
-
-
?
rac-4-methyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 100%
-
-
?
rac-4-nitro-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 32%
-
-
?
rac-4-nitro-hydroxy-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 61%
-
-
?
rac-4-propyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 126%
-
-
?
rac-4-trifluoromethyl-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 73%
-
-
?
rac-beta-leucine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 38%
-
-
?
rac-beta-phenylalanine + 2-oxoglutarate
?
show the reaction diagram
H8WR05
relative activity: 100%
-
-
?
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
?
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
?
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
?
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
-
-
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
no activity
-
-
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
62% of the activity than with L-tyrosine
-
?
L-tyrosine + pyruvate
?
show the reaction diagram
-, Q9LVY1
relative activity compared to 2-oxoglutarate: 40%
-
-
?
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
first step in tyrosine pathway leading to the formation of rosmarinic acid (alpha-O-caffeoyl-3,4-dihydroxyphenyllactic acid)
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
two mol coenzyme per mol of enzyme
pyridoxal 5'-phosphate
-
relative position of the cofactor at the active site determined by X-ray crystallography
pyridoxal 5'-phosphate
Q6GFC0
dependent
pyridoxal 5'-phosphate
-
dependent
pyridoxal 5'-phosphate
-
dependent
pyridoxal 5'-phosphate
-
dependent
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
H8WR05
-
pyridoxal 5'-phosphate
-
-
pyridoxamine 5'-phosphate
-
can replace pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Hg2+
-
a dose of 1-3 mg/kg increases the basal activity of the enzyme and decreases its induction by dexamethasone
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(4-hydroxyphenyl)acetic acid
-
74% inhibition with tyrosine at 3 mM and (4-hydroxyphenyl)acetic acid at 12 mM
2-aminooxyacetate
H8WR05
-
-
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
-
substrate inhibition at high concentration
2-oxoglutarate
H8WR05
enzyme shows substrate inhibition
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
AgNO3
-
10 mM, complete inhibition
alpha-Methyl-L-aspartate
-
with L-tyrosine and 2-oxoglutarate or oxaloacetate as substrates
alpha-Methyltyrosine
-
-
Aminooxyacetate
-
probably acts reacting with the cofactor
Aminooxyacetate
-
1 mM, complete inhibition
beta-Methyl-L-aspartate
-
with L-tyrosine and 2-oxoglutarate or oxaloacetate as substrates
beta-phenylalanine
H8WR05
enzyme shows substrate inhibition
-
Canaline
-
probably acts reacting with the cofactor
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
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
-
competitive inhibition
methiozolin
-
0.5 mM: 91% inhibition of enzyme activity, 0.25 mM: 57% inhibition of enzyme activity
-
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
adrenaline
-
activation is independent of the concentration of tyrosine, maximal activation achieved with 7-10 micromolar of adrenaline
dexamethasone
-
-
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
dopamine
-
slight activation
metanephrine
-
slight activation
noradrenaline
-
slight activation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.5
-
(S)-beta-phenylalanine
H8WR05
pH 7.6, 30C
-
0.13
-
2-Oxo-3-phenylpropanoate
-, Q9LVY1
pH 8.2, 30C
0.19
-
2-oxoglutarate
-, Q9LVY1
pH 8.2, 30C
0.25
-
2-oxoglutarate
-
pH 7.6, 37C
0.3
-
2-oxoglutarate
H8WR05
pH 7.6, 30C
0.35
-
2-oxoglutarate
P04694
mutant R315K, pH 7.5, 37C
0.35
-
2-oxoglutarate
-
pH 8.5, 30C
0.4
-
2-oxoglutarate
P04694
wild-type, pH 7.5, 37C
0.7
-
2-oxoglutarate
-
pH 7.2, 37C
0.9
-
2-oxoglutarate
-
pH 7.6, 37C, enzyme form I
1
-
2-oxoglutarate
-
pH 7.6, 37C, enzyme form III
1.1
-
2-oxoglutarate
-
pH 7.6, 37C, enzyme form II
1.2
-
2-oxoglutarate
-
pH 7.6, 37C, enzyme form IV
1.8
-
2-oxoglutarate
-
pH 7.0, 38C
3.5
-
2-oxoglutarate
P04694
mutant N54S, pH 7.5, 37C
4.6
-
2-oxoglutarate
P33447
wild-type, pH 7.5, 37C
9.6
-
2-oxoglutarate
P33447
mutant N17S, pH 7.5, 37C
14.8
-
2-oxoglutarate
P33447
mutant R20A, pH 7.5, 37C
38
-
2-oxoglutarate
-
pH 7.0, 37C, tyrosine as co-substrate
3300
-
2-oxoglutarate
-
wild type enzyme
7.3
-
2-Oxohexanoate
-
pH 7.0, 38C
0.3
-
2-oxoisocaproate
P33447
mutant R20A, pH 7.5, 37C
2.8
-
2-oxoisocaproate
P33447
mutant N17S, pH 7.5, 37C
20.4
-
2-oxoisocaproate
P33447
wild-type, pH 7.5, 37C
26
-
3,4-dihydroxyphenylalanine
-
pH 7.9, 37C
0.22
-
3-(4-hydroxyphenyl)-2-oxopropanoate
-, Q9LVY1
pH 8.2, 30C
0.7
-
4-hydroxyphenylpyruvate
-
pH 7.0, 38C
0.9
-
L-alanine
P33447
wild-type, pH 7.5, 37C
1.2
-
L-alanine
P33447
mutant N17S, pH 7.5, 37C; mutant R20A, pH 7.5, 37C
1.4
-
L-glutamate
-, Q9LVY1
pH 8.2, 30C
1.9
-
L-glutamate
P04694
mutant R315K, pH 7.5, 37C
2.2
-
L-glutamate
P04694
wild-type, pH 7.5, 37C
4.9
-
L-glutamate
-
pH 7.0, 38C
8.8
-
L-glutamate
P04694
mutant N54S, pH 7.5, 37C
0.84
-
L-phenylalanine
-, Q9LVY1
pH 8.2, 30C
6.33
-
L-phenylalanine
-
pH 8.5, 30C
11.4
-
L-phenylalanine
-
pH 7.0, 38C
7.83
-
L-tryptophane
-
pH 8.5, 30C
-
0.19
-
L-tyrosine
-, Q9LVY1
pH 8.2, 30C
0.21
-
L-tyrosine
-
aspartate aminotransferase with mutations HEX and I73V, A293D, pH 8.0, 25C
0.29
-
L-tyrosine
-
aspartate aminotransferase with mutations HEX and I73V, pH 8.0, 25C
0.33
-
L-tyrosine
-
aspartate aminotransferase with mutations HEX and A293D, pH 8.0, 25C
0.45
-
L-tyrosine
-
pH 9.2, 40C, isoenzyme TAT-3
0.5
-
L-tyrosine
-
pH 7.6, 37C
1.2
-
L-tyrosine
P33447
wild-type, pH 7.5, 37C
1.4
-
L-tyrosine
-
pH 7.6, 37C, enzyme form II
1.8
-
L-tyrosine
-
pH 7.0, 38C
1.82
-
L-tyrosine
-
pH 8.5, 30C
1.86
-
L-tyrosine
-
in liver
2.1
-
L-tyrosine
-
pH 7.6, 37C
2.1
-
L-tyrosine
P04694
wild-type, pH 7.5, 37C
2.3
-
L-tyrosine
P04694
mutant R315K, pH 7.5, 37C
2.3
-
L-tyrosine
P33447
mutant R20A, pH 7.5, 37C
2.4
-
L-tyrosine
P33447
mutant N17S, pH 7.5, 37C
2.5
5
L-tyrosine
-
in white muscle
3.4
-
L-tyrosine
-
pH 7.2, 37C
5
-
L-tyrosine
-
pH 9.2, 40C, isoenzyme TAT-2
5.3
-
L-tyrosine
P04694
mutant N54S, pH 7.5, 37C
6.8
-
L-tyrosine
-
pH 7.0, 37C, pyruvate as co-substrate
15
-
L-tyrosine
-
pH 7.9, 37C
20
-
L-tyrosine
-
pH 9.2, 40C, isoenzyme TAT-1
67
-
L-tyrosine
-
mutant enzyme I249A
16
-
oxaloacetate
-
pH 7.0, 37C, tyrosine as co-substrate
56.13
-
oxaloacetate
-
pH 8.5, 30C
1.2
-
p-hydroxyphenylpyruvate
P04694
mutant R315K, pH 7.5, 37C; wild-type, pH 7.5, 37C
1.3
-
p-hydroxyphenylpyruvate
P04694
mutant N54S, pH 7.5, 37C
580
-
p-hydroxyphenylpyruvate
-
wild type enzyme
17.9
-
phenylalanine
-
pH 7.0, 37C, pyruvate as co-substrate
80
-
phenylalanine
-
pH 7.9, 37C
0.9
-
phenylpyruvate
-
pH 7.0, 38C
0.5
-
pyruvate
-
pH 7.0, 37C, tyrosine as co-substrate
0.6
-
pyruvate
P33447
mutant N17S, pH 7.5, 37C; mutant R20A, pH 7.5, 37C
0.8
-
pyruvate
P33447
wild-type, pH 7.5, 37C
2.45
-
pyruvate
-
pH 8.5, 30C
21.4
-
tryptophan
-
pH 7.0, 37C, pyruvate as co-substrate
30
-
tryptophan
-
pH 7.9, 37C
60
-
tryptophan
-
pH 7.2, 37C
870
-
L-tyrosine
-
wild type enzyme
additional information
-
additional information
-
non-Michaelis complex kinetic
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
11.8
-
(S)-beta-phenylalanine
H8WR05
pH 7.6, 30C
-
0.22
-
2-oxoglutarate
-
pH 8.5, 30C
0.25
-
2-oxoglutarate
-
wild type enzyme
0.3
-
2-oxoglutarate
-
mutant enzyme I249A
0.5
-
2-oxoglutarate
P33447
mutant R20A, pH 7.5, 37C
4.2
-
2-oxoglutarate
P33447
mutant N17S, pH 7.5, 37C
10.6
-
2-oxoglutarate
H8WR05
pH 7.6, 30C
21.8
-
2-oxoglutarate
P33447
wild-type, pH 7.5, 37C
25.66
-
2-oxoglutarate
-
pH 7.0, 38C
116
-
2-oxoglutarate
P04694
mutant N54S, pH 7.5, 37C
490
-
2-oxoglutarate
P04694
mutant R315K, pH 7.5, 37C
566
-
2-oxoglutarate
P04694
wild-type, pH 7.5, 37C
1.83
-
2-Oxohexanoate
-
pH 7.0, 38C
0.4
-
2-oxoisocaproate
P33447
mutant R20A, pH 7.5, 37C
9.3
-
2-oxoisocaproate
P33447
mutant N17S, pH 7.5, 37C
34
-
2-oxoisocaproate
P33447
wild-type, pH 7.5, 37C
15.83
-
4-hydroxyphenylpyruvate
-
pH 7.0, 38C
0.35
-
L-alanine
P33447
mutant R20A, pH 7.5, 37C
3.8
-
L-alanine
P33447
mutant N17S, pH 7.5, 37C
23.5
-
L-alanine
P33447
wild-type, pH 7.5, 37C
3.8
-
L-glutamate
-
wild type enzyme
6.6
-
L-glutamate
P04694
mutant N54S, pH 7.5, 37C
9.33
-
L-glutamate
-
pH 7.0, 38C
69
-
L-glutamate
-
wild type enzyme
199
-
L-glutamate
P04694
mutant R315K, pH 7.5, 37C
210
-
L-glutamate
P04694
wild-type, pH 7.5, 37C
0.08
-
L-phenylalanine
-
pH 8.5, 30C
15.33
-
L-phenylalanine
-
pH 7.0, 38C
0.36
-
L-tryptophane
-
pH 8.5, 30C
-
0.24
-
L-tyrosine
-
pH 8.5, 30C
0.7
-
L-tyrosine
P33447
mutant R20A, pH 7.5, 37C
1
-
L-tyrosine
-
wild type enzyme
1.2
-
L-tyrosine
-
mutant enzyme I249A
1.8
-
L-tyrosine
P33447
mutant N17S, pH 7.5, 37C
19.33
-
L-tyrosine
-
pH 7.0, 38C
24
-
L-tyrosine
-
aspartate aminotransferase with mutations HEX, pH 8.0, 25C
25.6
-
L-tyrosine
-
aspartate aminotransferase with mutations HEX and I73V, pH 8.0, 25C
35.7
-
L-tyrosine
-
aspartate aminotransferase with mutations HEX and I73V, A293D, pH 8.0, 25C
39
-
L-tyrosine
-
aspartate aminotransferase with mutations HEX and A293D, pH 8.0, 25C
44.6
-
L-tyrosine
P33447
wild-type, pH 7.5, 37C
83
-
L-tyrosine
-
wild type enzyme
132
-
L-tyrosine
P04694
mutant N54S, pH 7.5, 37C
510
-
L-tyrosine
P04694
mutant R315K, pH 7.5, 37C
576
-
L-tyrosine
P04694
wild-type, pH 7.5, 37C
0.37
-
oxaloacetate
-
pH 8.5, 30C
1.2
-
p-hydroxyphenylpyruvate
-
wild type enzyme
5.9
-
p-hydroxyphenylpyruvate
P04694
mutant N54S, pH 7.5, 37C
155
-
p-hydroxyphenylpyruvate
P04694
mutant R315K, pH 7.5, 37C
165
-
p-hydroxyphenylpyruvate
P04694
wild-type, pH 7.5, 37C
2.66
-
phenylpyruvate
-
pH 7.0, 38C
0.34
-
pyruvate
-
pH 8.5, 30C
0.5
-
pyruvate
P33447
mutant R20A, pH 7.5, 37C
1.5
-
pyruvate
P33447
mutant N17S, pH 7.5, 37C
47.4
-
pyruvate
P33447
wild-type, pH 7.5, 37C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.63
-
2-oxoglutarate
-
pH 8.5, 30C
2883
14.16
-
2-oxoglutarate
-
pH 7.0, 38C
2883
0.33
-
2-Oxohexanoate
-
pH 7.0, 38C
2895
22.66
-
4-hydroxyphenylpyruvate
-
pH 7.0, 38C
4595
2
-
L-glutamate
-
pH 7.0, 38C
12211
0.01
-
L-phenylalanine
-
pH 8.5, 30C
12364
1.33
-
L-phenylalanine
-
pH 7.0, 38C
12364
0.05
-
L-tryptophane
-
pH 8.5, 30C
0
0.13
-
L-tyrosine
-
pH 8.5, 30C
12450
10.66
-
L-tyrosine
-
pH 7.0, 38C
12450
0.01
-
oxaloacetate
-
pH 8.5, 30C
14857
3
-
phenylpyruvate
-
pH 7.0, 38C
15509
0.14
-
pyruvate
-
pH 8.5, 30C
16065
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
82.4
-
2-oxoglutarate
H8WR05
enzyme shows substrate inhibition, pH 7.6, 30C
40.3
-
beta-phenylalanine
H8WR05
enzyme shows substrate inhibition, pH 7.6, 30C
-
20.3
-
L-glutamate
-
pH 7.6, 37C, isozyme I from kidney, L-tyrosine as substrate
26.8
-
L-glutamate
-
pH 7.6, 37C, isozyme IV from liver, L-tyrosine as substrate
27.4
-
L-glutamate
-
pH 7.6, 37C, isozyme III from liver, L-tyrosine as substrate
31.3
-
L-glutamate
-
pH 7.6, 37C, isozyme II from liver, L-tyrosine as substrate
additional information
-
additional information
-
inhibition due to L-glutamate
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
203
-
-
isoenzyme I
416
-
-
enzyme expressed in Escherichia coli
1200
-
-
from rats stimulated with corticosterone and dexamethasone
additional information
-
-
activities of different isoenzymes from liver, kidney and heart; effect of glucagon, cyclic nucletides, insulin and hydrocortisone on activity
additional information
-
-
-
additional information
-
-
effect of induction with hydrocortisone on activity
additional information
-
-
activities for different isoenzymes
additional information
-
-
-
additional information
-
-
-
additional information
-
-
effect of estradiol and ovariectomy on activity
additional information
-
-
effect of vitamin B-6 deficiency on activity
additional information
-
-
effect of induction with dexamethasone on activity
additional information
-
-
effect of induction with cAMP on activity
additional information
-
-
effect of acute and chronic ethanol administration on synthesis and activity of TAT
additional information
-
-
effect of chronic heat stress on activity
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
assay at
7.6
-
-
-
7.6
-
-
-
7.6
-
H8WR05
assay at
7.7
-
-
recombinant enzyme expressed in Escherichia coli
8.2
-
-, Q9LVY1
assay at
9
-
-
L-tyrosine as substrate, isoenzyme TAT-1
additional information
-
-
optimum pH for the isoenzyme TAT-2 is above pH 9.6
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
11.2
H8WR05
enzyme shows high activity over a broad pH range
8.8
9.4
-
L-tyrosine as substrate, isoenzyme TAT-3
additional information
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-, Q9LVY1
assay at
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
38
-
-
assay at
40
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
70
-
highest activity
55
-
-
decrease in activity above
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.25
-
Q6GFC0
2D-PAGE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
46420
-
H8WR05
calculated from cDNA
48170
-
Q6GFC0
X-ray crystallography
49600
-
-
calculated from amino acid sequence
50000
-
Q6GFC0
SDS-PAGE
85000
-
-
gel filtration, isoforms I and II
90000
-
-
amino acid composition and gel filtration
90000
-
-
isoenzymes: TAT-I, TAT-II, TAT-III, gel filtration
91000
-
-
gel filtration
100000
-
-
gel filtration
104500
-
-
ultracentrifugation
105000
-
-
glycerol gradient centrifugation
107000
-
-
gel filtration, different isoenzymes
110000
-
-
gel filtration
110000
-
-
recombinant expressed in Escherichia coli, ultracentrifugation
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
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 65000, SDS-PAGE
?
Q4E4E7
x * 42000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dimer
-
2 * 44000, isoenzymes TAT-I and TAT-II, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
Q6GFC0
S-75 gel filtration
heterodimer
-
1 * 50000 + 1 * 48000
monomer
-
1 * ?, SDS-PAGE
oligomer
-
? * 50000, SDS-PAGE
oligomer
-
x * 52000, SDS-PAGE
tetramer
-
4 * 43000, isoenzyme TAT-1, SDS-PAGE; 4 * 56000, isoenzyme TAT-2, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
not a glycoprotein
additional information
-
no measurable amount of fucose, mannose, galactose, N-acetylglucose, N-acetylgalactose nor sialic acid
proteolytic modification
-
liver isoform I is converted into functional lower molecular weight isoenzymes by a lysosomal convertase
additional information
-
not a glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
low resolution structure of the enzyme bound to pyridoxal 5'-phosphate
-
through macromolecular crystallography the mTAT crystal structure is determined at 2.9 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
H8WR05
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
15 min, 50% loss of activity, isoenzyme TAT-3
55
-
-
15 min, 50% loss of activity, isoenzyme TAT-2
60
-
-
stable below
65
-
-
15 min, 50% loss of activity, isoenzyme TAT-1
65
-
-
complete inactivation after 5 min
additional information
-
-
pyridoxal 5'-phosphate protects against thermal inactivation; the apoenzyme is thermally unstable: t1/2 of 2 min at 55C
additional information
-
-
2-oxoglutarate protects against thermal inactivation; pyridoxal 5'-phosphate protects against thermal inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-oxoglutarate protects against thermal inactivation
-
pyridoxal 5'-phosphate protects against thermal inactivation
-
sensitive to SH inactivation
-
pyridoxal 5'-phosphate protects against thermal inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 50 mM sodium phosphate, pH 6.5, 2 mM EDTA, 1 mM 2-mercaptoethanol, 2.5 mM 2-oxoglutarate
-
-20C, 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 ACCESSION NO.
LITERATURE
partial, using ammonium sulfate precipitation and several chromatographic steps
-
three isoenzymes TAT-1, TAT-2 and TAT-3, isolated using anion-exchange chromatography and electrofocusing
-
using Ni-NTA chromatography
-
partial
-
NTA-resin column chromatography
-
partial, using gel filtration
-
Ni-NTA column chromatography
-
using affinity, Source-Q and gel-filtration chromatography
-
partial purification of two isoenzymes, using several chromatographic steps
-
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
-
nickel Sepharose 6 fast flow chromatography, HiPrep 26/10 desalting column chromatography, and S-75 gel filtration
Q6GFC0
partial, using chromatography on DEAE-cellulose and gel filtration
-
using Ni-NTA chromatography
H8WR05
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
-, Q9LVY1
recombinantly expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21-CodonPlus (DE3)RIL cells
-
expressed in Escherichia coli
-
expression of rat liver enzyme in Saccharomyces cerevisiae and Escherichia coli
-
expressed in Escherichia coli
Q6GFC0
recombinantly expressed in Escherichia coli as a His-tagged fusion protein
H8WR05
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
P04694
reduced enzymic activity
R315K
P04694
retains enzymic activity
R417Q
P04694
no enzymic activity
R57A
P04694
no enzymic activity
R57Q
P04694
no enzymic activity
N17S
P33447
increase in Km-values, substantial decrease in kcat-values
R20A
P33447
increase in Km-values, substantial decrease in kcat-values
R41A
H8WR05
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
Q4E4E7
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