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Literature summary for 2.6.1.5 extracted from

  • Rothman, S.C.; Voorhies, M.; Kirsch, J.F.
    Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase (2004), Protein Sci., 13, 763-772.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.5

Protein Variants

Protein Variants Comment Organism
additional information switch of aspartate aminotransferase to use of tyrosine substrate by introduction of six mutations obtained by rational design and termed HEX plus mutation A293D or mutation I73V Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.21
-
 L-tyrosine aspartate aminotransferase with mutations HEX and I73V, A293D, pH 8.0, 25°C Escherichia coli
0.29
-
 L-tyrosine aspartate aminotransferase with mutations HEX and I73V, pH 8.0, 25°C Escherichia coli
0.33
-
 L-tyrosine aspartate aminotransferase with mutations HEX and A293D, pH 8.0, 25°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tyrosine + 2-oxoglutarate
-
 Escherichia coli 4-hydroxyphenylpyruvate + L-glutamate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
24
-
 L-tyrosine aspartate aminotransferase with mutations HEX, pH 8.0, 25°C Escherichia coli
25.6
-
 L-tyrosine aspartate aminotransferase with mutations HEX and I73V, pH 8.0, 25°C Escherichia coli
35.7
-
 L-tyrosine aspartate aminotransferase with mutations HEX and I73V, A293D, pH 8.0, 25°C Escherichia coli
39
-
 L-tyrosine aspartate aminotransferase with mutations HEX and A293D, pH 8.0, 25°C Escherichia coli