Specificity of Proteinase K at P₂ to P₃’ Sub-sites and its Comparison to other Serine Proteases

Title:Specificity of Proteinase K at P₂ to P₃’ Sub-sites and its Comparison to other Serine Proteases

Volume: 21 Issue: 2

Author(s): Mohammad A. Qasim

Affiliation:

Keywords: Protease specificity, proteinase K, serine proteases, standard mechanism inhibitor, subtilisins, turkey ovomucoid third domain.

Abstract: Specificity of the commercially important serine protease, proteinase K, has been investigated by measuring free energies of association of proteinase K with turkey ovomucoid third domain inhibitor variants at contact positions P₂, P₁, P₁', P₂', and P₃'. Correlations of these values were run with similar values that have been obtained for six other serine proteases. Among the six proteases, subtilisin Carlsberg shows a near perfect correlation (Pearson Product correlation coefficient = 0.93 to 0.99) with proteinase K at all of these positions. Proteinase K has only 35% sequence identity with subtilisin Carlsberg, yet, the two enzymes are nearly identical in their specificity at P₂ to P₃' positions. With other serine proteases such as bovine chymotrypsin, human leukocyte elastase, porcine pancreatic elastase, Streptomyces griseus protease A and B, proteinase K showed relatively poor or no correlation.

Cite this article as:

Qasim A. Mohammad, Specificity of Proteinase K at P₂ to P₃’ Sub-sites and its Comparison to other Serine Proteases, Protein & Peptide Letters 2014; 21 (2) . https://dx.doi.org/10.2174/09298665113206660093

DOI https://dx.doi.org/10.2174/09298665113206660093	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305