Moriyama R, Kudoh S, Miyata S, Nonobe S, Hattori A, Makino S
Department of Applied Biological Sciences, School of Agricultural Sciences, Nagoya University, Japan.
J Bacteriol. 1996 Sep;178(17):5330-2. doi: 10.1128/jb.178.17.5330-5332.1996.
A gene (sleB) encoding a 24-kDa germination-specific spore cortex-lytic enzyme, probably an N-acetylmuramyl-L-alanine amidase, was cloned from Bacillus cereus, and its nucleotide sequence was determined. It was indicated that the enzyme is produced as a 259-residue protein with a signal sequence of 32 residues and is present in dormant spores in its active form. Sulfhydryl reagents inactivated the enzyme, but mutation of a single cysteine of the protein, Cys-258, to Gly did not cause complete inactivation of the enzyme, suggesting that the residue does not function as the catalytic center of enzyme.
从蜡状芽孢杆菌中克隆出一个编码24 kDa萌发特异性芽孢皮层裂解酶的基因(sleB),该酶可能是一种N-乙酰胞壁酰-L-丙氨酸酰胺酶,并测定了其核苷酸序列。结果表明,该酶以含有32个氨基酸残基信号序列的259个氨基酸残基蛋白质形式产生,并以其活性形式存在于休眠芽孢中。巯基试剂可使该酶失活,但将蛋白质中的单个半胱氨酸残基Cys-258突变为甘氨酸并不会导致该酶完全失活,这表明该残基并非该酶的催化中心。