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2.6.1.5: tyrosine transaminase

This is an abbreviated version!
For detailed information about tyrosine transaminase, go to the full flat file.

Word Map on EC 2.6.1.5

Reaction

L-tyrosine
+
2-oxoglutarate
=
4-hydroxyphenylpyruvate
+
L-glutamate

Synonyms

aminotransferase, tyrosine, At5g36160, At5g53970, beta-phenylalanine aminotransferase, glutamic phenylpyruvic aminotransferase, glutamic-hydroxyphenylpyruvic transaminase, L-phenylalanine 2-oxoglutarate aminotransferase, L-tyrosine aminotransferase, L-tyrosine-2-oxoglutarate aminotransferase, L-tyrosine: 2 oxoglutarate aminotransferase, L-tyrosine: 2-oxoglutarate aminotransferase, More, mTAT, phenylalanine aminotransferase, phenylalanine transaminase, phenylalanine-alpha-ketoglutarate transaminase, phenylpyruvate transaminase, phenylpyruvic acid transaminase, PPY-AT, Sar2028, TAT, TAT1, TAT2, TAT3, TATase, TATc, Tyr aminotransferase, TyrAT, tyrosine aminotransferase, tyrosine-2-ketoglutarate aminotransferase, tyrosine-2-oxoglutarate aminotransferase, tyrosine-alpha-ketoglutarate aminotransferase, tyrosine-alpha-ketoglutarate transaminase, VpAT

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.5 tyrosine transaminase

Crystallization

Crystallization on EC 2.6.1.5 - tyrosine transaminase

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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
A0A163U8E7
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