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Literature summary for 2.6.1.1 extracted from

  • Chow, M.A.; McElroy, K.E.; Corbett, K.D.; Berger, J.M.; Kirsch, J.F.
    Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase (2004), Biochemistry, 43, 12780-12787.
    View publication on PubMed
Search for more literature for 2.6.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals are grown at 19°C by the hanging-drop technique, unliganded and hydrocinnamate complex of V39L/K41Y/T47I/N69L/T109S/A293D/N297S, hydrocinnamate complex and maleate complexes of A12T/P13T/N34D/T109S/G261A/S285G/N297S and the hydrocinnamate complex of A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S Escherichia coli

Protein Variants

Protein Variants Comment Organism
A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S mutant enzyme has nearly the same ratio of kcat/Km(Phe) to kcat/Km(Asp) as that of wild-type enzyme. The additional mutation A293D compared to mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/N297S holds the Arg292 side chain away from the active site to allow increased specificity for phenylalanine over aspartate Escherichia coli
V39L/K41Y/T47I/N69L/T109S/A293D/N297S the additional mutation A293D compared to mutant enzyme V39L/K41Y/T47I/N69L/T109S/N297S holds the Arg292 side chain away from the active site to allow increased specificity for phenylalanine over aspartate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.3
-
 L-Phe pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S Escherichia coli
0.48
-
 2-oxoglutarate pH 8, cosubstrate: L-Phe, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S Escherichia coli
2.6
-
 2-oxoglutarate pH 8, cosubstrate: L-Asp, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S Escherichia coli
29
-
 L-Asp pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P00509
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
 Escherichia coli oxaloacetate + L-glutamate
-
 ?
L-Phe + 2-oxoglutarate
-
 Escherichia coli 2-oxo-3-phenylpropionic acid + L-glutamate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
10
-
 L-Phe pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S Escherichia coli
43
-
 L-Asp pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S Escherichia coli