Usui M, Sembongi H, Matsuzaki H, Matsumoto K, Shibuya I
Department of Biochemistry, Saitama University, Urawa, Japan.
J Bacteriol. 1994 Jun;176(11):3389-92. doi: 10.1128/jb.176.11.3389-3392.1994.
The nucleotide sequence of the Escherichia coli pgsA gene, encoding phosphatidylglycerophosphate synthase, is revised to code for an enzyme of 182 amino acid residues, instead of the 216 of a previous work (A. S. Gopalakrishnan, Y.-C. Chen, M. Temkin, and W. Dowhan, J. Biol. Chem. 261:1329-1338, 1986). The revised structure now explains the properties of the enzyme. Three pgsA mutants of different phenotypes were also analyzed: pgsA3, pgsA36, and pgsA10 have single-base replacements in codons 60 (Thr-->Pro), 1 (ATG-->ATA), and 92 (Thr-->Ile), respectively.
编码磷脂酰甘油磷酸合酶的大肠杆菌pgsA基因的核苷酸序列经修订后编码一种由182个氨基酸残基组成的酶,而非先前研究(A. S. 戈帕拉克里什南、Y.-C. 陈、M. 坦金和W. 多曼,《生物化学杂志》261:1329 - 1338, 1986)中所报道的216个氨基酸残基。修订后的结构如今解释了该酶的特性。还对三个不同表型的pgsA突变体进行了分析:pgsA3、pgsA36和pgsA10分别在密码子60(苏氨酸→脯氨酸)、1(ATG→ATA)和92(苏氨酸→异亮氨酸)处发生了单碱基替换。