Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg
نویسندگان
چکیده
منابع مشابه
Acylation of subtilisin Carlsberg by phenyl esters.
Approximate Hammett reaction constants rho calculated from k2/K8 values of several phenyl esters of N-acetyl-L-phenylalanine, hippuric acid, and beta-phenylpropionic acid are 0.0, 0.4, and 1.0 respectively. To determine whether the lack of substituent effect of k2/K8 with the N-acetyl-L-phenylalanine esters is a result of substituent-insensitive k2 or rate-limiting association of enzyme and sub...
متن کاملSubtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships.
Evidence is presented for the complete amino acid sequence of subtilisin Carlsberg. The protein consists of a single peptide chain of 274 residues. Comparison with subtilisin BPN’ shows 84 amino acid differences and 1 additional residue in BPN’. The 84 differences can be accounted for on the basis of single or double nucleotide replacements. Within the subtilisins, there are a number of distinc...
متن کاملObtaining higher transesterification rates with subtilisin Carlsberg in nonaqueous media.
Three phase partitioning (protein precipitate obtained as an interfacial layer between lower aqueous and upper t-butanol phases, formed by the addition of ammonium sulphate and t-butanol to the aqueous solution of protein) followed by lyophilization in the presence of two-component excipient resulted in 400-480x increases in transesterification activity of lyophilized powders of subtilisin Carl...
متن کاملThe crystal structure of subtilisin Carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile.
The x-ray crystal structure of the serine protease subtilisin Carlsberg in anhydrous dioxane has been determined to 2.6-A resolution. The enzyme structure is found to be nearly indistinguishable from the structures previously determined in water and acetonitrile. Small changes in the side-chain conformations between the dioxane and water structures are of the same magnitude as those observed be...
متن کاملImmobilization of Subtilisin Carlsberg on Modified Silica Gel by Cross-linking and Covalent Binding Methods
Proteases are important enzymes that their role in various industries is undeniable. However, keeping enzymes stable during its activity in harsh conditions is so important. In this study, protease enzyme was immobilized on the porous silica particles and its stability in different temperatures and pHs was evaluated. First silica particles were aminated by 3-aminopropyltriethoxysilane then the ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1998
ISSN: 0014-2956,1432-1033
DOI: 10.1046/j.1432-1327.1998.2570309.x