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Information on EC 2.6.1.5 - tyrosine transaminase and Organism(s) Trypanosoma cruzi and UniProt Accession P33447

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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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Trypanosoma cruzi
UNIPROT: P33447
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The taxonomic range for the selected organisms is: Trypanosoma cruzi
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
aminotransferase, tyrosine
-
-
-
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glutamic phenylpyruvic aminotransferase
-
-
-
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glutamic-hydroxyphenylpyruvic transaminase
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-
-
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L-phenylalanine 2-oxoglutarate aminotransferase
-
-
-
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L-tyrosine aminotransferase
-
-
-
-
L-tyrosine-2-oxoglutarate aminotransferase
-
-
-
-
phenylalanine aminotransferase
-
-
-
-
phenylalanine transaminase
-
-
-
-
phenylalanine-alpha-ketoglutarate transaminase
-
-
-
-
phenylpyruvate transaminase
-
-
-
-
phenylpyruvic acid transaminase
-
-
-
-
tyrosine aminotransferase
-
-
-
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tyrosine-2-ketoglutarate aminotransferase
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-
-
-
tyrosine-2-oxoglutarate aminotransferase
-
-
-
-
tyrosine-alpha-ketoglutarate aminotransferase
-
-
-
-
tyrosine-alpha-ketoglutarate transaminase
-
-
-
-
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-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoisocaproate
pyruvate + 2-aminoisocaproate
show the reaction diagram
-
-
-
?
L-tyrosine + pyruvate
4-hydroxyphenylpyruvate + L-alanine
show the reaction diagram
-
-
-
?
L-glutamate + oxaloacetate
L-aspartate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
L-glutamate + pyruvate
L-alanine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 2-oxoglutarate
L-glutamate + phenylpyruvate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
relative position of the cofactor at the active site determined by X-ray crystallography
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.6 - 14.8
2-oxoglutarate
0.3 - 20.4
2-oxoisocaproate
0.9 - 1.2
L-alanine
1.2 - 2.4
L-tyrosine
0.6 - 0.8
pyruvate
38
2-oxoglutarate
-
pH 7.0, 37°C, tyrosine as co-substrate
17.9
L-phenylalanine
-
pH 7.0, 37°C, pyruvate as co-substrate
6.8
L-tyrosine
-
pH 7.0, 37°C, pyruvate as co-substrate
16
oxaloacetate
-
pH 7.0, 37°C, tyrosine as co-substrate
0.5
pyruvate
-
pH 7.0, 37°C, tyrosine as co-substrate
21.4
tryptophan
-
pH 7.0, 37°C, pyruvate as co-substrate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 21.8
2-oxoglutarate
0.4 - 34
2-oxoisocaproate
0.35 - 23.5
L-alanine
0.7 - 44.6
L-tyrosine
0.5 - 47.4
pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Swissprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ATTY_TRYCR
416
0
46167
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
x * 42000, SDS-PAGE
45000
-
2 * 45000, SDS-PAGE
91000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 42000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
not a glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure determined at 2.5 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N17S
increase in Km-values, substantial decrease in kcat-values
R20A
increase in Km-values, substantial decrease in kcat-values
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
complete inactivation after 5 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial, using chromatography on DEAE-cellulose and gel filtration
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Montemartini, M.; Santome, J.A.; Cazzulo, J.J.; Nowick, C.
Purification and partial structural and kinetic characterization of tyrosine aminotransferase from epimastigotes of Trypanosoma cruzi
Biochem. J.
292
901-906
1993
Trypanosoma cruzi
Manually annotated by BRENDA team
Blankenfeldt, W.; Nowicki, C.; Montemartini-Kalisz, M.; Kalisz, H.M.; Hecht, H.J.
Crystal structure of Trypanosoma cruzi tyrosine aminotransferase: substrate specificity is influenced by cofactor binding mode
Protein Sci.
8
2406-2417
1999
Trypanosoma cruzi
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
Rego, J.V.; Murta, S.M.; Nirde, P.; Nogueira, F.B.; de Andrade, H.M.; Romanha, A.J.
Trypanosoma cruzi: characterisation of the gene encoding tyrosine aminotransferase in benznidazole-resistant and susceptible populations
Exp. Parasitol.
118
111-117
2008
Trypanosoma cruzi (Q4E4E7), Trypanosoma cruzi
Manually annotated by BRENDA team