Thermal and Pressure Inactivation of 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 کاملComparative studies of the specificities of -chymotrypsin and subtilisin BPN'. Studies with flexible and 'locked' substrates.
Subtilisin BPN' hydrolysed N-acetyl-l-3-(2-naphthyl)-alanine methyl ester, N-acetyl-l-leucine methyl ester and N-acetyl-l-valine methyl ester, faster than alpha-chymotrypsin. Of eight ;locked' substrates tested, only methyl 5,6-benzindan-2-carboxylate was hydrolysed faster by subtilisin, whereas the other esters were better substrates for chymotrypsin. Compared with the values for chymotrypsin,...
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...
متن کاملStructural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'.
The crystal structures of two thermally stabilized subtilisin BPN' variants, S63 and S88, are reported here at 1.8 and 1.9 A resolution, respectively. The micromolar affinity calcium binding site (site A) has been deleted (Delta75-83) in these variants, enabling the activity and thermostability measurements in chelating conditions. Each of the variants includes mutations known previously to inc...
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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ژورنال
عنوان ژورنال: Journal of the Society of Materials Science, Japan
سال: 1996
ISSN: 1880-7488,0514-5163
DOI: 10.2472/jsms.45.274