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2.6.1.57: aromatic-amino-acid transaminase

This is an abbreviated version!
For detailed information about aromatic-amino-acid transaminase, go to the full flat file.

Word Map on EC 2.6.1.57

Reaction

an aromatic amino acid
+
2-oxoglutarate
=
an aromatic oxo acid
 +
L-glutamate

Synonyms

AAT, AAT I-III, AAT1, aminotransferase, aromatic amino acid, ArAT, ArAT-I, ArAT-ITL, ArATPf, ArATPh, Aro8, ARO9, AroAT, AroAT II, AroATEs, AroH, arom. amino acid transferase, arom.-amino-acid transaminase, aromatic amino acid aminotransferase, aromatic amino acid transaminase, aromatic amino transferase I, aromatic aminotransferase, aromatic aminotransferase AT-1, aromatic aminotransferase AT-2, aromatic aminotransferase II, aromatic L-amino acid transaminase, aromatic-amino-acid aminotransferase, aromatic-amino-acid:2-oxoglutarate transaminase, AT-1, AT-2, AT-IA, At1g80360, bifunctional 2-aminoadipate transaminase/aromatic-amino-acid:2-oxoglutarate transaminase, CaAro8p, CaAro9p, CaYer152Cp, eAroATEs, F5I6.11, hisC1, indole severe sensitive 1, ISS1, More, pdArAT, pdAroAT, PH1371, phhC, PjAT, SmAroAT, TyrB, TyrB-2, VAT1, Yer152, Yer152C

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.57 aromatic-amino-acid transaminase

Engineering

Engineering on EC 2.6.1.57 - aromatic-amino-acid transaminase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y66A
-
kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 43.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 51.5fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 558fold lower than wild-type value
Y66F
-
kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 2.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 3.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 4.5fold lower than wild-type value
Y66L
-
mutant enzyme is able to synthesize L-diphenylalanine with 23% conversion yield for 10 h, whereas the wild-type AroATEs is inactive for the transamination between diphenylpyruvate and L-phenylalanine. kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 2.65fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 3.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 4.9fold lower than wild-type value
Y66V
-
kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 26.5fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 23.1fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 558fold lower than wild-type value
Y66A
-
kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 43.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 51.5fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 558fold lower than wild-type value
-
Y66F
-
kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 2.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 3.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 4.5fold lower than wild-type value
-
Y66L
-
mutant enzyme is able to synthesize L-diphenylalanine with 23% conversion yield for 10 h, whereas the wild-type AroATEs is inactive for the transamination between diphenylpyruvate and L-phenylalanine. kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 2.65fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 3.4fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 4.9fold lower than wild-type value
-
Y66V
-
kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Phe as substrate is 26.5fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Asp as substrate is 23.1fold lower than wild-type value, kcat for the reaction with 2-oxo-4-phenylbutyrate and L-Glu as substrate is 558fold lower than wild-type value
-
K258A
-
pKa of the Schiff base formed between the coenzyme pyridoxal 5'-phosphate and Lys258 increases by 3.6 units
R292A
R292K
-
very low activity with aspartate, 10-100fold increase in Km for aromatic amino acids
R292L
R386L
-
pKa of the Schiff base formed between the coenzyme pyridoxal 5'-phosphate and Lys258 increases by 0.7 units
nutrition
-
enzyme and branched chain amino acid transaminase are essential for conversion of aromatic and branched-chain amino acids to aroma compounds in the cheese model and also play a major role in the formation of volatile sulfur compounds from methionine
additional information