Kim J C, Cha S H, Jeong S T, Oh S K, Byun S M
Department of Life Science, Korea Advanced Institute of Science and Technology, Yuseong-Gu, Taejon.
Biochem Biophys Res Commun. 1991 Dec 16;181(2):707-13. doi: 10.1016/0006-291x(91)91248-b.
Streptomyces griseus trypsin (E.C. 3.4.21.4) is one of the major extracellular proteinase, which is secreted by S. griseus. The gene encoding S. griseus trypsin was isolated from a S. griseus genomic library by using a synthetic oligonucleotide probe. Fragments containing the gene for S. griseus trypsin were characterized by hybridization and demonstration of proteolytic activity in S. lividans. Deduced amino acid sequence from the nucleotide sequence suggests that S. griseus trypsin is produced as a precursor, consisting of three portions; an amino-terminal pre sequence (32 amino acid residues), a pro sequence (4 residues), and the mature trypsin. The S. griseus trypsin consists of 223 amino acids with a computed molecular weight of 23,112. The existence of proline at the pro and mature junction suggests that the processing of S. griseus trypsin is non-autocatalytic.
灰色链霉菌胰蛋白酶（E.C. 3.4.21.4）是灰色链霉菌分泌的主要细胞外蛋白酶之一。通过使用合成寡核苷酸探针从灰色链霉菌基因组文库中分离出编码灰色链霉菌胰蛋白酶的基因。通过杂交和在变铅青链霉菌中证明蛋白水解活性来表征含有灰色链霉菌胰蛋白酶基因的片段。从核苷酸序列推导的氨基酸序列表明，灰色链霉菌胰蛋白酶以前体形式产生，由三部分组成；氨基末端前序列（32个氨基酸残基）、前肽序列（4个残基）和成熟胰蛋白酶。灰色链霉菌胰蛋白酶由223个氨基酸组成，计算分子量为23,112。前肽和成熟肽连接处脯氨酸的存在表明灰色链霉菌胰蛋白酶的加工是非自催化的。
