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Literature summary for 6.1.1.22 extracted from

  • Madern, D.; Anselme, J.; Härtlein, M.
    Asparaginyl-tRNA synthetase from the Escherichia coli temperature-sensitive strain HO202. A proline replacement in motif 2 is responsible for a large increase in Km for asparagine and ATP (1992), FEBS Lett., 299, 85-89.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
P231L temperature-sensitive mutant HO202, P231L replacement leads to a change in aminoacylation activity. 50fold increased Km for Asn compared to the wild-type, and 8fold increase for ATP in ATP-diphosphate exchange. Significantly increased Km-values for Asn and ATP in aminoacylation. Pro-231 does not seem to be implicated directly in substrate binding. Instead it seems to have a structural role on the positioning of the loop formed by the motif 2 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.015
-
Asn wild-type, 37°C, ATP-diphosphate exchange Escherichia coli
0.029
-
Asn wild-type, 25°C, aminoacylation Escherichia coli
0.032
-
Asn wild-type, 37°C, aminoacylation Escherichia coli
0.076
-
ATP wild-type, 37°C, aminoacylation Escherichia coli
0.09
-
Asn mutant P231L, 25°C, aminoacylation Escherichia coli
0.094
-
Asn mutant P231L, 25°C, ATP-diphosphate exchange Escherichia coli
0.33
-
Asn mutant P231L, 37°C, aminoacylation Escherichia coli
0.5
-
ATP wild-type, 37°C, ATP-diphosphate exchange Escherichia coli
0.77
-
Asn mutant P231L, 37°C, ATP-diphosphate exchange Escherichia coli
0.87
-
ATP mutant P231L, 25°C, ATP-diphosphate exchange Escherichia coli
1
-
ATP mutant P231L, 37°C, aminoacylation Escherichia coli
4
-
ATP mutant P231L, 37°C, ATP-diphosphate exchange Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
wild-type and temperature-sensitive mutant HO202
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-asparagine + tRNAAsn
-
Escherichia coli AMP + diphosphate + L-asparaginyl-tRNAAsn
-
?
additional information ATP-diphosphate exchange Escherichia coli ?
-
?

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
mutant enzyme P231L has reduced activity at 30°C compared with the wild-type Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.3
-
ATP mutant P231L, 37°C, aminoacylation Escherichia coli
0.9
-
Asn mutant P231L, 37°C, aminoacylation Escherichia coli
1
-
Asn mutant P231L, 37°C, ATP-diphosphate exchange Escherichia coli
1.3
-
ATP wild-type, 37°C, aminoacylation Escherichia coli
1.3
-
ATP mutant P231L, 25°C, ATP-diphosphate exchange Escherichia coli
1.6
-
Asn wild-type, aminoacylation Escherichia coli
1.6
-
Asn 37°C Escherichia coli
2
-
ATP mutant P231L, 37°C, ATP-diphosphate exchange Escherichia coli
2.2
-
ATP wild-type, 37°C, ATP-diphosphate exchange Escherichia coli
2.2
-
Asn mutant P231L, 25°C, aminoacylation Escherichia coli
2.8
-
Asn wild-type, 37°C, ATP-diphosphate exchange Escherichia coli
2.8
-
Asn wild-type, 25°C, aminoacylation Escherichia coli
3
-
Asn mutant P231L, 25°C, ATP-diphosphate exchange Escherichia coli