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Literature summary for 2.6.1.1 extracted from

  • Deu, E.; Koch, K.A.; Kirsch, J.F.
    The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variants (2002), Protein Sci., 11, 1062-1073.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.1

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type enzyme and mutants from plasmid in Escherichia coli strain MG204, which lacks endogenous enzyme activity Escherichia coli

Protein Variants

Protein Variants Comment Organism
E265K site-directed mutagenesis, reduced kcat, reduced Km for L-aspartate and 2-oxoglutarate Escherichia coli
E265Q site-directed mutagenesis, reduced kcat, reduced Km for L-aspartate and 2-oxoglutarate Escherichia coli
K68E site-directed mutagenesis, reduced kcat, reduced Km for L-aspartate and increased Km for 2-oxoglutarate Escherichia coli
K68E/E265K site-directed mutagenesis, charge exchange in the conserved intrasubunit salt bridge, reduced kcat, reduced Km for L-aspartate and 2-oxoglutarate Escherichia coli
K68M site-directed mutagenesis, reduced kcat, reduced Km for L-aspartate and increased Km for 2-oxoglutarate Escherichia coli
K68M/E265Q site-directed mutagenesis, introduction of a neutral amino acid pair in the conserved intrasubunit salt bridge, reduced kcat, reduced Km for L-aspartate and 2-oxoglutarate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics Escherichia coli
additional information
-
 additional information mutants Escherichia coli
0.59
-
 2-oxoglutarate wild-type, pH 8.4, 25°C Escherichia coli
1.9
-
 L-aspartate wild-type, pH 8.4, 25°C Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate + 2-oxoglutarate Escherichia coli
-
 oxaloacetate + L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutants from overexpressing strain MG204 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
 Escherichia coli oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate
-
 Escherichia coli oxaloacetate + L-glutamate
-
 r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information mutants Escherichia coli
259
-
 L-aspartate wild-type, pH 8.4, 25°C Escherichia coli