Takagi J S, Tokushige M, Shimura Y, Kanehisa M
Biochem Biophys Res Commun. 1986 Jul 31;138(2):568-72. doi: 10.1016/s0006-291x(86)80534-4.
Based on our recent determinations of the nucleotide sequences of the L-aspartate ammonia-lyase genes from Escherichia coli and Pseudomonas fluorescens, primary structures of the two L-aspartate ammonia-lyases and fumarate hydratases from Bacillus subtilis and E. coli (N-terminal partial sequence) were compared by computer analysis. These four enzymes exhibited a significant homology of at least 37%, implying that L-aspartate ammonia-lyase and fumarate hydratase share a common evolutionary origin. To authors' knowledge, this feature appears to be the first example showing that two kinds of enzymes catalyzing different types of reactions, albeit similar, share such a high degree of sequence homology.
基于我们最近对来自大肠杆菌和荧光假单胞菌的L-天冬氨酸氨裂解酶基因核苷酸序列的测定,通过计算机分析比较了来自枯草芽孢杆菌和大肠杆菌的两种L-天冬氨酸氨裂解酶以及富马酸水合酶的一级结构(N端部分序列)。这四种酶显示出至少37%的显著同源性,这意味着L-天冬氨酸氨裂解酶和富马酸水合酶有着共同的进化起源。据作者所知,这一特征似乎是首个表明两种催化不同类型反应(尽管相似)的酶具有如此高度序列同源性的例子。