EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
6.1.1.3 | H73A | site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme, and a 2fold higher rate of ATP consumption relative to the rate of Ser-tRNAThr synthesis | Escherichia coli |
6.1.1.3 | H73A/H309A | site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme, and a 2fold higher rate of ATP consumption relative to the rate of Ser-tRNAThr synthesis | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.3 | Mg2+ | required | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.3 | ATP + L-threonine + tRNAThr | Escherichia coli | - |
AMP + diphosphate + L-threonyl-tRNAThr | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.1.1.3 | Escherichia coli | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.3 | ATP + L-threonine + tRNAThr | - |
Escherichia coli | AMP + diphosphate + L-threonyl-tRNAThr | - |
? | |
6.1.1.3 | additional information | in the pre-steady state, asymmetric activation of cognate threonine and noncognate serine is observed in the active sites of dimeric ThrRS, with similar rates of activation. In the absence of tRNA, seryl-adenylate is hydrolyzed 29old faster by the ThrRS catalytic domain than threonyl-adenylate. The rate of seryl transfer to cognate tRNA is only 2fold slower than threonine | Escherichia coli | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.1.1.3 | dimer | - |
Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.1.1.3 | More | the enzyme belongs to the class II aminoacyl-tRNA synthetases | Escherichia coli |
6.1.1.3 | Threonyl-tRNA synthetase | - |
Escherichia coli |
6.1.1.3 | ThrRS | - |
Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.1.1.3 | 37 | - |
assay at | Escherichia coli |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.1.1.3 | additional information | - |
additional information | rate constants for adenylate synthesis by ThrRS in the absence of tRNA, overview | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
6.1.1.3 | 8 | - |
assay at | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.3 | ATP | - |
Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
6.1.1.3 | physiological function | amino acid discrimination does not occur at the aminoacyl transfer step. pre-Transfer hydrolysis contributes to proofreading only when the rate of transfer is slowed significantly. Thus, the relative contributions of pre- and posttransfer editing in ThrRS are subject to modulation by the rate of aminoacyl transfer | Escherichia coli |