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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

Engineering

Engineering on EC 2.6.1.5 - tyrosine transaminase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
reduced enzymic activity
R315K
retains enzymic activity
R417Q
no enzymic activity
R57A
no enzymic activity
R57Q
no enzymic activity
N17S
increase in Km-values, substantial decrease in kcat-values
R20A
increase in Km-values, substantial decrease in kcat-values
R41A
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