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Literature summary for 2.6.1.1 extracted from

  • Lo, H.H.; Hsu, S.K.; Lin, W.D.; Chan, N.L.; Hsu, W.H.
    Asymmetrical synthesis of L-homophenylalanine using engineered Escherichia coli aspartate aminotransferase (2005), Biotechnol. Prog., 21, 411-415.
    View publication on PubMed
Search for more literature for 2.6.1.1

Application

Application Comment Organism
synthesis mutant enzyme R292E/L18H can use L-lysine as inexpensive amino donor for the production of L-homophenylalanine. The low solubility of product L-homophenylalanine and spontaneous cyclization of 2-keto-6-aminocaproate drive the reaction completely towards production of L-homophenylalanine Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
R292E/L18H 12.9fold increase in specific activity towards L-Lys and 2-oxo-4-phenylbutanoic acid Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.77
-
 2-oxo-4-phenyl-butanoic acid wild-type enzyme Escherichia coli
0.86
-
 2-oxo-4-phenyl-butanoic acid mutant enzyme R292E/L18H Escherichia coli
105
-
 L-Lys mutant enzyme R292E/L18H Escherichia coli
189
-
 L-Lys wild-type enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Lys + 2-oxo-4-phenyl-butanoic acid mutant enzyme R292E/L18H shows a 12.9fold increase in specific activity towards L-Lys and 2-oxo-4-phenylbutanoic acid Escherichia coli L-homophenylalanine + 2-keto-6-aminocaproate 2-keto-6-aminocaproate is cyclized nonenzymatically to form DELTA1-piperideine 2-carboxylic acid in the reaction mixture. The low solubility of L-homophenylalanine and spontaneous cyclization of 2-keto-6-aminocaproate drive the reaction completely towards production of L-homophenylalanine ?

Synonyms

Synonyms Comment Organism
AAT
-
 Escherichia coli
aspartate aminotransferase
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.305
-
 L-Lys wild-type enzyme Escherichia coli
0.35
-
 2-oxo-4-phenyl-butanoic acid wild-type enzyme Escherichia coli
0.38
-
 2-oxo-4-phenyl-butanoic acid mutant enzyme R292E/L18H Escherichia coli
5.55
-
 L-Lys mutant enzyme R292E/L18H Escherichia coli