Taguchi S, Odaka A, Watanabe Y, Momose H
Department of Biological Science and Technology, Science University of Tokyo, Chiba, Japan.
Appl Environ Microbiol. 1995 Jan;61(1):180-6. doi: 10.1128/aem.61.1.180-186.1995.
An extracellular serine protease produced by a mutant, M1, derived from Streptomyces albogriseolus S-3253 that no longer produces a protease inhibitor (Streptomyces subtilisin inhibitor [SSI]) was isolated. A 20-kDa protein was purified by its affinity for SSI and designated SAM-P20. The amino acid sequence of the amino-terminal region of SAM-P20 revealed high homology with the sequences of Streptomyces griseus proteases A and B, and the gene sequence confirmed the relationships. The sequence also revealed a putative amino acid signal sequence for SAM-P20 that apparently functioned to allow secretion of SAM-P20 from Escherichia coli carrying the recombinant gene. SAM-P20 produced by E. coli cells was shown to be sensitive to SSI inhibition.
从不再产生蛋白酶抑制剂（链霉菌枯草杆菌蛋白酶抑制剂[SSI]）的白灰链霉菌S-3253衍生的突变体M1中分离出一种细胞外丝氨酸蛋白酶。一种20 kDa的蛋白质通过其对SSI的亲和力被纯化，并命名为SAM-P20。SAM-P20氨基末端区域的氨基酸序列与灰色链霉菌蛋白酶A和B的序列具有高度同源性，基因序列证实了这种关系。该序列还揭示了SAM-P20的一个推定氨基酸信号序列，其明显起到使携带重组基因的大肠杆菌分泌SAM-P20的作用。大肠杆菌细胞产生的SAM-P20显示对SSI抑制敏感。
