Title

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

Document Type

Article

Publication Date

2-2014

Publication Source

Protein and Peptide Letters

Volume

21

Issue

2

Inclusive pages

164-170

Peer Reviewed

yes

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.

Keywords

Protease specificity; Proteinase K; Serine proteases; Standard Mechanism Inhibitor; Subtilisins; Turkey Ovomucoid Third Domain

Disciplines

Biochemistry | Chemistry

This document is currently not available here.

  Contact Author

Share

COinS