Specificity of proteinase K at P2 to P3' sub-sites and its comparison to other serine proteases.
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.
Department of Chemistry, 2101 E. Coliseum Blvd., Indiana University Purdue University, Fort Wayne, IN 46805, USA. qasimm@ipfw.edu.
Mohammad A
MA
Qasim
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D019286:Endopeptidase K / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D013045:Species Specificity; D013379:Substrate Specificity; D014359:Trypsin Inhibitor, Kazal Pancreatic / Q000494:pharmacology
D015842:Serine Proteinase Inhibitors; C039345:ovomucoid inhibitors; D014359:Trypsin Inhibitor, Kazal Pancreatic; D019286:Endopeptidase K