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