title: Substrate specificity of alkaline proteases from Cephalosporium sp. KM388.
abstract: Serine alkaline proteases from Cephalosporium sp. KM388 were specific against esters of aromatic and hydrophobic amino acids. Against oxidized insulin B-chain, the enzymes initially cleaved the site of Leu-Tyr(15-16). The cleavage specificity of KM388 protease D was broader than those of other alkaline proteases, and the site of Arg-Gly(22-23) was cleaved, which is a specific site for trypsin-like protease.
authors.affiliation: Faculty of Pharmaceutical Sciences, Josai University, Saitama, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Tsuchiya
authors.forename: K
authors.initials: K
authors.lastname: Seki
authors.forename: T
authors.initials: T
authors.lastname: Arai
authors.forename: T
authors.initials: T
authors.lastname: Masui
mesh_terms: D000164:Acremonium / Q000201:enzymology*; D000595:Amino Acid Sequence; D001665:Binding Sites; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D012697:Serine Endopeptidases