Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | 3-hydroxynorvaline enhances the ATPase function of the synthetic site, at a rate not increased by nonaminoacylatable tRNA | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
expression of His-tagged ThrRS | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | pre-steady-state kinetics, kinetics of ATPase activity in presence of 3-hydroxynorvaline, overview | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-threonine + tRNAThr | Escherichia coli | - |
AMP + diphosphate + L-threonyl-tRNAThr | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged ThrRS by nickel affinity chromatography | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 3-hydroxynorvaline + tRNAThr | the specificity constant kcat/KM for beta-hydroxynorvaline is only 20-30fold less than that of cognate threonine, amino acid activation is the potential rate-limiting step of b3-hydroxynorvaline aminoacylation | Escherichia coli | AMP + diphosphate + 3-hydroxynorvalyl-tRNAThr | - |
? | |
ATP + L-threonine + tRNAThr | - |
Escherichia coli | AMP + diphosphate + L-threonyl-tRNAThr | - |
? | |
ATP + L-threonine + tRNAThr | for cognate threonine, amino acid activation is likely to be the rate-limiting step. The inability of wild-type ThrRS to prevent utilization of beta-hydroxynorvaline as a substrate illustrates that the naturally occurring enzyme lacks the capability to effectively discriminate against nonproteogenic amino acids that are not encountered under normal physiological conditions | Escherichia coli | AMP + diphosphate + L-threonyl-tRNAThr | - |
? |
Synonyms | Comment | Organism |
---|---|---|
More | the enzyme belongs to the class II aminoacyl-tRNA synthetases | Escherichia coli |
Threonyl-tRNA synthetase | - |
Escherichia coli |
ThrRS | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |