鼠伤寒沙门氏菌两种磷酸酶和一种环磷酸二酯酶的特性
Properties of two phosphatases and a cyclic phosphodiesterase of Salmonella typhimurium.
作者信息
Weppelman R, Kier L D, Ames B N
出版信息
J Bacteriol. 1977 Apr;130(1):411-9. doi: 10.1128/jb.130.1.411-419.1977.
The properties of three phosphatases from Salmonella typhimurium have been examined. A cyclic 2',3'-nucleotide phosphodiesterase (EC 3.1.4.d) hydrolyzes cyclic 2',3'-purine and -pyrimidine nucleotides, as well as 3'-mononucleotides, and has a pH optimum of about 7.5. It requires divalent cations for activity and has a molecular weight of 67,000. Acid hexose phosphatase (EC 3.1.2.2) possesses activity towards hexose phosphates as well as other sugar phosphates. The enzyme is apparently a dimer of 37,000-dalton subunits. Nonspecific acid phosphatase (EC 3.1.3.2) hydrolyzes a variety of phosphate esters, including nucleotides and sugar phosphates. The enzyme also hydrolyzes the phosphoric anhydride bonds of pyrophosphate and nucleotides. Michaelis constants of the nonspecific acid phosphatase for several of its substrates are in the 1 to 2 mM range. Nonspecific acid phosphatase is a dimer of 27,000-dalton subunits.
对鼠伤寒沙门氏菌的三种磷酸酶的特性进行了研究。一种环2',3'-核苷酸磷酸二酯酶（EC 3.1.4.d）可水解环2',3'-嘌呤和嘧啶核苷酸以及3'-单核苷酸，其最适pH约为7.5。它的活性需要二价阳离子，分子量为67,000。酸性己糖磷酸酶（EC 3.1.2.2）对己糖磷酸以及其他糖磷酸具有活性。该酶显然是由37,000道尔顿亚基组成的二聚体。非特异性酸性磷酸酶（EC 3.1.3.2）可水解多种磷酸酯，包括核苷酸和糖磷酸。该酶还可水解焦磷酸和核苷酸的磷酸酐键。非特异性酸性磷酸酶对其几种底物的米氏常数在1至2 mM范围内。非特异性酸性磷酸酶是由27,000道尔顿亚基组成的二聚体。
Zotero 插件