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Literature summary for 2.6.1.57 extracted from

  • Cho, B.K.; Seo, J.H.; Kang, T.J.; Kim, J.; Park, H.Y.; Lee, B.S.; Kim, B.G.
    Engineering aromatic L-amino acid transaminase for the asymmetric synthesis of constrained analogs of L-phenylalanine (2006), Biotechnol. Bioeng., 94, 842-850.
    View publication on PubMed
Search for more literature for 2.6.1.57

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Enterobacter sp.

Protein Variants

Protein Variants Comment Organism
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 Enterobacter sp.
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 Enterobacter sp.
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 Enterobacter sp.
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 Enterobacter sp.

Organism

Organism UniProt Comment Textmining
Enterobacter sp.
-
 BK2K-1
-
Enterobacter sp. BK2K-1
-
 BK2K-1
-

Purification (Commentary)

Purification (Comment) Organism
-
 Enterobacter sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxo-4-phenylbutyrate + L-Asp
-
 Enterobacter sp. 2-amino-4-phenylbutyrate + oxaloacetate
-
 ?
2-oxo-4-phenylbutyrate + L-Asp
-
 Enterobacter sp. BK2K-1 2-amino-4-phenylbutyrate + oxaloacetate
-
 ?
2-oxo-4-phenylbutyrate + L-Glu
-
 Enterobacter sp. 2-amino-4-phenylbutyrate + 2-oxoglutarate
-
 ?
2-oxo-4-phenylbutyrate + L-Glu
-
 Enterobacter sp. BK2K-1 2-amino-4-phenylbutyrate + 2-oxoglutarate
-
 ?
2-oxo-4-phenylbutyrate + L-Phe
-
 Enterobacter sp. 2-amino-4-phenylbutyrate + phenylpyruvate
-
 ?
2-oxo-4-phenylbutyrate + L-Phe
-
 Enterobacter sp. BK2K-1 2-amino-4-phenylbutyrate + phenylpyruvate
-
 ?
diphenylpyruvate + L-phenylalanine Y66L AroATEs produces enantiomerically pure L-diphenylalanine with 23% conversion yield for 10 h, whereas Y66A, Y66V, and Y66F AroATEs are not able to catalyze the transamination reaction. The Y66F and Y66L AroATEs show amino donor specificity toward L-phenylalanine with 42% and 38% enzymatic activity of the wild-type AroATEs, respectively. The forward half-reaction between L-phenylalanine and PLP is observed with the mutant enzymes Y66F and Y66L AroATEs. The backward half-reaction between diphenylpyruvate and PMP enzyme is only detected with Y66L AroATEs Enterobacter sp. L-diphenylalanine + phenylpyruvate
-
 ?
diphenylpyruvate + L-phenylalanine Y66L AroATEs produces enantiomerically pure L-diphenylalanine with 23% conversion yield for 10 h, whereas Y66A, Y66V, and Y66F AroATEs are not able to catalyze the transamination reaction. The Y66F and Y66L AroATEs show amino donor specificity toward L-phenylalanine with 42% and 38% enzymatic activity of the wild-type AroATEs, respectively. The forward half-reaction between L-phenylalanine and PLP is observed with the mutant enzymes Y66F and Y66L AroATEs. The backward half-reaction between diphenylpyruvate and PMP enzyme is only detected with Y66L AroATEs Enterobacter sp. BK2K-1 L-diphenylalanine + phenylpyruvate
-
 ?

Synonyms

Synonyms Comment Organism
aromatic L-amino acid transaminase
-
 Enterobacter sp.
eAroATEs
-
 Enterobacter sp.