Subtilisin secreted from a variety of Bacillus species is an alkaline protease. The peptide-chain folding of this kind of enzyme is totally different from the mammalian serine protease, but their catalytic residues ar...Subtilisin secreted from a variety of Bacillus species is an alkaline protease. The peptide-chain folding of this kind of enzyme is totally different from the mammalian serine protease, but their catalytic residues are the same and have almost identical space arrangement, so they belong to different kinds of serine proteases. The structure and function of subtilisin have been studied extensively. Subtilisin also has some other advantages for protein engineering studies and is an important industrial enzyme which is mass-used as a component of synthetic detergent to degrade proteins. Therefore a展开更多
Animal lysozymes can selectively cleave a kind of glycosidic bond ofN-acetylglucosamine in the bacterial cell wall peptidoglycan. The hen egg-white lysozymeconsists of a single polypeptide chain containing 129 amino a...Animal lysozymes can selectively cleave a kind of glycosidic bond ofN-acetylglucosamine in the bacterial cell wall peptidoglycan. The hen egg-white lysozymeconsists of a single polypeptide chain containing 129 amino acid residues and fourdisulfide bonds. The three-dimensional structure of this enzyme was determined展开更多
基金Project supported by the National High-Tech. Program of China.
文摘Subtilisin secreted from a variety of Bacillus species is an alkaline protease. The peptide-chain folding of this kind of enzyme is totally different from the mammalian serine protease, but their catalytic residues are the same and have almost identical space arrangement, so they belong to different kinds of serine proteases. The structure and function of subtilisin have been studied extensively. Subtilisin also has some other advantages for protein engineering studies and is an important industrial enzyme which is mass-used as a component of synthetic detergent to degrade proteins. Therefore a
基金Project supported by the National High-Tech Program of China.
文摘Animal lysozymes can selectively cleave a kind of glycosidic bond ofN-acetylglucosamine in the bacterial cell wall peptidoglycan. The hen egg-white lysozymeconsists of a single polypeptide chain containing 129 amino acid residues and fourdisulfide bonds. The three-dimensional structure of this enzyme was determined
