Protein Variants | Comment | Organism |
---|---|---|
additional information | mutations within the amino acid sequence alpha17-40 influence the organic co-solvent-induced conformation and concomittant resistance of E30-R31 peptide bond to cleavage occurs, alteration of the thermaldynamic stability of the splicedon, the flanking regions are involved in stabilization | Staphylococcus aureus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics and thermodynamic stability | Staphylococcus aureus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Staphylococcus aureus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
human hemoglobin + H2O | slpicedon consisting of a flanking region FR1, the EALER sequence, and a flanking region FR2, splicing reaction at E30-R31, facilitated by organic co-solvent-induced secondary conformation of alpha17-40 within which the sequence EALER plays a major role | Staphylococcus aureus | ? | - |
? | |
additional information | splicing activity and specificity of the enzyme with complementary segments of human hemoglobin fragment alpha17-40, constructed by engineering of the primary structure, structural implications, overview | Staphylococcus aureus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
V8 protease | - |
Staphylococcus aureus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
4 | - |
assay at | Staphylococcus aureus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Staphylococcus aureus |