Cloned (Comment) | Organism |
---|---|
complementatiom of a growth mutant defective in phenylalanylation in vivo by wild-type full-length PheRS from Saccharomyces cerevisiae, the full-length Escherichia coli enzyme A294G, and the truncated mutant PheRSDELTAB2, overexpression of full-length mutant A294G and truncated mutant PheRSDELTAB2A294G in strain XL-1 Blue | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
A294G | thermosensitive active site mutant strain NP37 enzyme | Escherichia coli |
additional information | construction of a truncated mutant PheRSDELTAB2A294G, lacking the B2 domain, which shows kinetics for in vitro aminoacylation comparable to the wild-type enzyme, a 2-fold drop compared to full-length PheRS in the catalytic efficiency of Tyr-tRNAPhe hydrolysis | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | full-length PheRSA294G and truncated mutant PheRSDELTAB2A294G show comparable kinetics for in vitro aminoacylation, kinetics, overview | Escherichia coli | |
0.0022 | - |
tRNAPhe | pH 7.2, 37°C, full-length PheRSA294G, substrate from Saccharomyces cerevisiae | Escherichia coli | |
0.0025 | - |
tRNAPhe | pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Escherichia coli | Escherichia coli | |
0.0027 | - |
tRNAPhe | pH 7.2, 37°C, full-length PheRSA294G, substrate from Escherichia coli | Escherichia coli | |
0.0041 | - |
tRNAPhe | pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Saccharomyces cerevisiae | Escherichia coli | |
0.0049 | - |
L-phenylalanine | pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G | Escherichia coli | |
0.0053 | - |
L-phenylalanine | pH 7.2, 37°C, full-length PheRSA294G | 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 | the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? | |
ATP + L-phenylalanine + tRNAPhe | Escherichia coli NP37 | the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
carrying the thermosensitive point mutation A294G in the active site | - |
Escherichia coli NP37 | - |
carrying the thermosensitive point mutation A294G in the active site | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-phenylalanine + tRNAPhe | the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis | Escherichia coli | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? | |
ATP + L-phenylalanine + tRNAPhe | a two-step reaction, tRNAPhe substrate from Escherichia coli and Saccharomyces cerevisiae, the enzyme contains the dispensable B2 RNA-binding domain that contributes to the post-transfer editing of noncognate aminoacyl-tRNA, the B2 domain does not enhance tRNA folding, overview | Escherichia coli | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? | |
ATP + L-phenylalanine + tRNAPhe | the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis | Escherichia coli NP37 | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? | |
ATP + L-phenylalanine + tRNAPhe | a two-step reaction, tRNAPhe substrate from Escherichia coli and Saccharomyces cerevisiae, the enzyme contains the dispensable B2 RNA-binding domain that contributes to the post-transfer editing of noncognate aminoacyl-tRNA, the B2 domain does not enhance tRNA folding, overview | Escherichia coli NP37 | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? |
Subunits | Comment | Organism |
---|---|---|
oligomer | PheRs is a multidomain (alphabeta)2 heterotetrameric protein, the alpha subunit forms the catalytic core of the enzyme, while the beta subunit contains a number of autonomous structural modules with a wide range of functions including tRNA anticodon binding and editing of the misaminoacylated species Tyr-tRNAPhe | 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 | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.077 | - |
tRNAPhe | pH 7.2, 37°C, full-length PheRSA294G, substrate from Saccharomyces cerevisiae | Escherichia coli | |
0.11 | - |
tRNAPhe | pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Saccharomyces cerevisiae | Escherichia coli | |
0.78 | - |
tRNAPhe | pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Escherichia coli | Escherichia coli | |
0.82 | - |
tRNAPhe | pH 7.2, 37°C, full-length PheRSA294G, substrate from Escherichia coli | Escherichia coli | |
3.27 | - |
L-phenylalanine | pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G | Escherichia coli | |
3.34 | - |
L-phenylalanine | pH 7.2, 37°C, full-length PheRSA294G | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |