Title: On the Evolution of Specificity and Catalysis in Subtilisin
Abstract:Serine proteases are present in almost all organisms and exhibit a wide range of substrate specificities (for reviews, see Stroud 1974; Kraut 1977). The enzymes are characterized by a set of three cat...Serine proteases are present in almost all organisms and exhibit a wide range of substrate specificities (for reviews, see Stroud 1974; Kraut 1977). The enzymes are characterized by a set of three catalytic residues consisting of a serine, a histidine, and an aspartic acid (the catalytic triad). Nature has apparently evolved the catalytic triad structure and the resulting serine protease mechanism at least twice. In particular, subtilisin (from species of bacillus) and chymotrypsin (from mammalian pancreas) are genetically unrelated and their corresponding tertiary structures are entirely different. However, it is possible to virtually superimpose the catalytic triad and some features of the substrate-binding site from these convergently related enzymes (Kraut et al. 1971).Read More
Publication Year: 1987
Publication Date: 1987-01-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
Access and Citation
Cited By Count: 7
AI Researcher Chatbot
Get quick answers to your questions about the article from our AI researcher chatbot