Akiyama M, Crooke E, Kornberg A
Department of Biochemistry, Stanford University School of Medicine, California 94305-5307.
J Biol Chem. 1993 Jan 5;268(1):633-9.
A gene, ppx, that encodes a novel exopolyphosphatase of 513 amino acids (58,133 Da) was found downstream of the gene for polyphosphate kinase, ppk. Transcription of the ppx gene depends on the ppk promoters, indicating a polyphosphate (polyP) operon of ppk and ppx. Exopolyphosphatase, purified to homogeneity from overproducing cells, is judged to be a dimer of 58-kDa subunits. Orthophosphate is released processively from the ends of polyP approximately 500 residues long, but chains of approximately 15 residues compete poorly with polyP as substrate; ATP is not a substrate. Mg2+ (1 mM) and a high concentration of K+ (175 mM) support optimal activity.
在编码多聚磷酸激酶(ppk)的基因下游发现了一个名为ppx的基因,它编码一种由513个氨基酸(58,133道尔顿)组成的新型外切多聚磷酸酶。ppx基因的转录依赖于ppk启动子,这表明存在一个由ppk和ppx组成的多聚磷酸盐(polyP)操纵子。从过量表达的细胞中纯化至同质的外切多聚磷酸酶被判定为58-kDa亚基的二聚体。正磷酸盐从大约500个残基长的多聚磷酸链末端逐步释放,但大约15个残基的链作为底物与多聚磷酸的竞争能力较差;ATP不是底物。Mg2+(1 mM)和高浓度的K+(175 mM)支持最佳活性。