Title: Inhibition ofAspergillusSerine Proteinase byStreptomycesSubtilisin Inhibitor and High-Level Expression of This Inhibitor inPichia pastoris
Abstract: Aspergillus fumigatusencodes an extracellular serine proteinase of the subtilisin family that is thought to be involved in invasive aspergillus infection of immunocompromised patients. When the structure of proteinase K was used to model thisAspergillusserine proteinase,Streptomycessubtilisin inhibitor (SSI) was predicted to be capable of binding to the serine proteinase. SSI purified fromS. albogriseolusinhibited the serine proteinase with Kiof 1 × 10−9M. This value is higher than that for subtilisin probably because the serine proteinase lacks the S4–6site that interacts with the P4–6site of SSI. A high level expression for SSI, established inPichia pastoris,yielded 0.5g of SSI per liter of culture medium. The secreted product was easily purified to homogeneity and biochemically characterized. The recombinant SSI showed a Kiof 1.1 × 10−9and 1 × 10−8for the serine proteinases fromA. fumigatusandA. flavus,respectively.
Publication Year: 1996
Publication Date: 1996-03-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 8
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