The gene, ialA, associated with the invasion of human erythrocytes by Bartonella bacilliformis, designates a nudix hydrolase active on dinucleoside 5′-polyphosphates
The gene, ialA, associated with the invasion of human erythrocytes by Bartonella bacilliformis, designates a nudix hydrolase active on dinucleoside 5′-polyphosphates
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DOI：
10.1074/jbc.274.3.1203
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发表时间：
1999-01-15
影响因子：
4.8
通讯作者：
Bessman, MJ
中科院分区：
文献类型：
--
作者：
Conyers, GB;Bessman, MJ
iaLA是与杆状巴尔通体（Bartonella bacilliformis）侵入人红细胞相关的两个基因之一，杆状巴尔通体是几种疾病的病原体，iaLA已经在大肠杆菌中被克隆并抑制。蛋白质IalA含有一系列酶的氨基酸序列特征，即对多种核苷二磷酸衍生物具有活性的NuI水解酶。IalA已被纯化、鉴定和表征为催化一类信号核苷酸（多磷酸二核苷）成员水解的酶，其对腺苷5’-四磷酸-5’-腺苷（Ap（4）A）具有最高活性，但也水解Ap（5）A、Ap（6）A、Gp（4）G和Gp（5）G。在每种情况下，焦磷酸键被裂解，产生核苷三磷酸和剩余的核苷酸部分。
iaLA, one of two genes associated with the invasion of human red blood cells by Bartonella bacilliformis, the causative agent of several diseases, has been cloned and depressed in Escherichia coli. The protein, IalA, contains an amino acid array characteristic of a family of enzymes, the Nudix hydrolases, active on a variety of nucleoside diphosphate derivatives. IalA has been purified, identified, and characterized as an enzyme catalyzing the hydrolysis of members of a class of signaling nucleotides, the dinucleoside polyphosphates, with its highest activity on adenosine 5'-tetraphospho-5'-adenosine (Ap(4)A), but also hydrolyzing Ap(5)A, Ap(6)A, Gp(4)G, and Gp(5)G. In each case, a pyrophosphate linkage is cleaved yielding a nucleoside triphosphate and the remaining nucleotide moiety.