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Literature summary for 3.4.21.62 extracted from

  • Abdizadeh, H.; Guven, G.; Atilgan, A.R.; Atilgan, C.
    Perturbation response scanning specifies key regions in subtilisin serine protease for both function and stability (2015), J. Enzyme Inhib. Med. Chem., 30, 867-873.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
G166R the mutant is both more stable and displays more activity compared to the wild-type enzyme Bacillus licheniformis
S161C the mutant brings increased stability to subtilisin compared to the wild-type Bacillus licheniformis

Inhibitors

Inhibitors Comment Organism Structure
additional information molecular dynamics simulations, residue displacement correlations, and inhibitor design based on the enzyme inhibitor comlpex of TI-II and subtilisin, overview Bacillus licheniformis
tomato inhibitor-II TI-II, enzyme binding structure, the interdomain interface in TI-II consists of a small cluster of highly conserved hydrophobic residues Ile14, Pro16, Tyr98, Phe100 and Phe106 from domain I and Tyr34, Pro54 and Lys55 from domain II. Although this interface is quite small (buried surface area of 487A), it forms a stable packing arrangement between the two domains. Each reactive site loop in TI-II interacts with a separate molecule of subtilisin in the canonical manner observed in other proteinase–inhibitor complexes. The domains of TI-II appear to bind the proteinase independently of each other Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
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Synonyms

Synonyms Comment Organism
subtilisin Carlsberg
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Bacillus licheniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
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assay at Bacillus licheniformis