Subtilisin Novo. The Three-Dimensional Structure and Its Comparison with Subtilisin BPN'
نویسندگان
چکیده
منابع مشابه
Subtilisin 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 کاملX-ray Crystallographic Study of Boronic Acid Adducts with Subtilisin BPN’ (Novo)
We have studied the structures of adducts formed between subtilisin BPN’ and both benzeneboronic acid and Z-phenylethaneboronic acid by x-ray diffraction techniques. Electron density and difference maps at 2.5 A resolution were computed with phases calculated from a partially refined structure of the native enzyme (R = 0.23 at 2.0 A). Both adducts contain a covalent bond between 07 of the catal...
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We have studied the structures of adducts formed between subtilisin BPN' and both benzeneboronic acid and 2-phenylethaneboronic acid by x-ray diffraction techniques. Electron density and difference maps at 2.5 A resolution were computed with phases calculated from a partially refined structure of the native enzyme (R = 0.23 at 2.0 A). Both adducts contain a covalent bond between Ogamma of the c...
متن کاملSubstrate Specificity of Aqualysin I, a Bacterial Thermophilic Alkaline Serine Protease from Thermus aquaticus YT-1: Comparison with Proteinase K, Subtilisin BPN' and Subtilisin Carlsberg.
Aqualysin I is the alkaline serine protease isolated from an extreme thermophile, Thermus aquaticus YT-1. We analyzed kinetic properties of aqualysin I, using sixteen kinds of chromogenic succinyl-tripeptide p-nitroanilides as substrates. And we compared the substrate specificity of aqualysin I with those of proteinase K, subtilisin BPN', and subtilisin Carlsberg. We found that aqualysin I had ...
متن کاملMolecular recognition at the active site of subtilisin BPN': crystallographic studies using genetically engineered proteinaceous inhibitor SSI (Streptomyces subtilisin inhibitor).
Unlike trypsin-like serine proteases having only one conspicuous binding pocket in the active site, subtilisin BPN' has two such pockets, the S1 and S4 pockets, which accommodate the P1 and P4 residues of ligands (after Schechter and Berger notation) respectively. Using computer graphics, the geometrical nature of the two pockets was carefully examined and strategies for site-directed mutagenes...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1972
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1972.tb01754.x