Protein Variants | Comment | Organism |
---|---|---|
N280S | the mutant displays wild-type aminoacylation activity and stability with respect to their free energies of unfolding, but are less stable at low pH. It shows no significant loss in secondary structure. The mutant retains less activity than wild-type enzyme after refolding for mitochondrial import | Homo sapiens |
S57C | the mutant displays wild-type aminoacylation activity and stability with respect to their free energies of unfolding, but are less stable at low pH. It shows no significant loss in secondary structure. The mutant retains less activity than wild-type enzyme after refolding for mitochondrial import | Homo sapiens |
S57C/N280S | Ser57 and Asn280 map to positions away from the catalytic center and the anticodon binding domain of hmtPheRS, the mutant does not show significant loss in secondary structure or aminoacylation activity in vitro compared to wild-type enzyme. The S57C/N280S double mutant had remarkable stability even at low pH | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Homo sapiens | 5739 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
More | structure molecular dynamics simulations of hmtPheRS, wild-type and mutant enzymes, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
mtPheRS | - |
Homo sapiens |
Phenylalanyl-tRNA synthetase | - |
Homo sapiens |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
1.5 | 8 | high stability of wild-type and mutant mtPheRSs in the pH range, unfolding parameters, overview | Homo sapiens |