Protein Variants | Comment | Organism |
---|---|---|
additional information | editing-defective PheRS variants display significantly increased tyrosylation levels in the presence of EF-Tu, likely through elongation factor Tu, EF-Tu, protection of synthesized Tyr-tRNAPhe from hydrolysis, overview | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | aminoacylation kinetics with Phe and Tyr | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-phenylalanine + tRNAPhe | Escherichia coli | cognate amino acid charging | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? | |
ATP + L-tyrosine + tRNAPhe | Escherichia coli | PheRS misactivates Tyr but is able to correct the mistake using a proofreading editing activity, overview, after evading editing by PheRS, Tyr-tRNAPhe is recognized by elongation factor Tu EF-Tu, involved in translational quality control including substrate selection by aminoacyl-tRNA synthetases, as efficiently as the cognate Phe-tRNAPhe, overview | AMP + diphosphate + L-tyrosinyl-tRNAPhe | - |
? | |
additional information | Escherichia coli | PheRS editing is the major proofreading step that prevents infiltration of Tyr into Phe codons during translation | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-phenylalanine + tRNAPhe | cognate amino acid charging | Escherichia coli | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? | |
ATP + L-phenylalanine + tRNAPhe | cognate amino acid charging onto tRNAPheUUU and tRNAPheUUC | Escherichia coli | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? | |
ATP + L-tyrosine + tRNAPhe | PheRS misactivates Tyr but is able to correct the mistake using a proofreading editing activity, overview, after evading editing by PheRS, Tyr-tRNAPhe is recognized by elongation factor Tu EF-Tu, involved in translational quality control including substrate selection by aminoacyl-tRNA synthetases, as efficiently as the cognate Phe-tRNAPhe, overview | Escherichia coli | AMP + diphosphate + L-tyrosinyl-tRNAPhe | - |
? | |
additional information | PheRS editing is the major proofreading step that prevents infiltration of Tyr into Phe codons during translation | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Phenylalanyl-tRNA synthetase | - |
Escherichia coli |
PheRS | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at, aminoaclyation | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
assay at, aminoaclyation | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |