Protein Variants | Comment | Organism |
---|---|---|
C5A/C49A | site-directed mutagenesis, the folding of the mutant lacking the disulfide bond is impaired and conformational stability is decreased compared to the wild-type enzyme, mutEcoAcP folds about 1500fold slower and a partially folded species accumulates int he mutant expressing strain | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics and thermodynamics of wild-type and mutant enzymes,overview | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0AB65 | - |
- |
Renatured (Comment) | Organism |
---|---|
folding and unfolding kinetics of wild-type and mutant enzymes at 28°C and pH 5.5 as a function of GdnHCl concentration, overview | Escherichia coli |
Subunits | Comment | Organism |
---|---|---|
More | structure determination and protein folding analysis of wild-type and mutant enzymes by far-UV and near-UV circular dichroism and dynamic light-scattering measurements, the protein folding of AcP is enhanced by disulfide bonds, overview | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
ACP | - |
Escherichia coli |