Crystallization (Comment) | Organism |
---|---|
structure of the processed protein is determined at 2.6 A resolution and compared with that of the full-length protein, in which the N-terminal extension binds back over the active site. A conserved proline introduces a backbone kink that shifts the scissile bond beyond reach of the catalytic serine and in addition the catalytic triad is disrupted. In the processed form, access to the active site is unblocked by removal of the N-terminal extension and the catalytic triad rearranges to a functional conformation | Alkalihalobacillus clausii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
N1-18[ISP] | synthetic peptide corresponding to the N-terminal extension behaves as a mixed noncompetitive inhibitor of active ISP | Alkalihalobacillus clausii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
31550 | - |
mass spectroscopy, processed form | Alkalihalobacillus clausii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alkalihalobacillus clausii | D0AB41 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | prosequence regulates ISP activity through two distinct modes: active site blocking and catalytic triad rearrangement. The full-length proenzyme is inactive until specific proteolytic processing removes the first 18 amino acids that comprise the N-terminal extension, with processing appearing to be performed by ISP itself | Alkalihalobacillus clausii |
Synonyms | Comment | Organism |
---|---|---|
intracellular subtilisin protease | - |
Alkalihalobacillus clausii |
ISP | - |
Alkalihalobacillus clausii |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.001 | - |
N1-18[ISP] | synthetic peptide corresponding to the N-terminal extension behaves as a mixed noncompetitive inhibitor of active ISP, pH and temperature not specified in the publication | Alkalihalobacillus clausii |