Cloned (Comment) | Organism |
---|---|
subtilisin variants expressed in Escherichia coli | Bacillus amyloliquefaciens |
Crystallization (Comment) | Organism |
---|---|
1.8 A resolution structure of an inactive form (by replacing the catalytic nucleophile Ser 221 with alanine) of the protease subtilisin S189, in complex with azide and with a prodomain substrate that spans the active site. The substrate is well ordered across the active site, and the azide anion is observed bound adjacent to Ala 32. Although S189, like wild-type subtilisin, has Ser as the catalytic nucleophile at residue 221, these crystal structures have Ala 221 to prevent cleavage of the substrate | Bacillus amyloliquefaciens |
Protein Variants | Comment | Organism |
---|---|---|
A1C | does not change the catalytic properties of subtilisin S189 but allows the introduction of a fluorescent group at its N-terminus | Bacillus amyloliquefaciens |
D32A | engineered variant of the protease subtilisin, denoted S189, mutation renders the enzyme's activity dependent on the presence of certain small anions such as fluoride or azide. Is activated more than 3000fold by azide | Bacillus amyloliquefaciens |
S221A | inactive form of subtilisin S189 | Bacillus amyloliquefaciens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus amyloliquefaciens | P00782 | - |
- |
Purification (Comment) | Organism |
---|---|
by affinity purification, more than 95% pure | Bacillus amyloliquefaciens |
Synonyms | Comment | Organism |
---|---|---|
subtilisin | - |
Bacillus amyloliquefaciens |