Solaroli Nicola, Panayiotou Christakis, Johansson Magnus, Karlsson Anna
Department of Laboratory Medicine, Karolinska Institute, Huddinge, Sweden.
FEBS Lett. 2009 Sep 3;583(17):2872-6. doi: 10.1016/j.febslet.2009.07.047. Epub 2009 Aug 3.
A full length cDNA that partially corresponded to human adenylate kinase 5 (AK5) was identified and shown to encode for two separate domains. The full length protein could be divided in two distinct functional domains, a previously unidentified domain of 338 amino acids and a second domain of 198 amino acids that corresponded to the protein characterized as AK5, now called AK5p2. The first domain, AK5p1, phosphorylated AMP, CMP, dAMP and dCMP with ATP or GTP as phosphate donors similarly to AK5p2. Our data demonstrate that human AK5 has two separate functional domains and that both have enzymatic activity.
鉴定出一段与人类腺苷酸激酶5（AK5）部分对应的全长cDNA，并显示其编码两个独立的结构域。全长蛋白可分为两个不同的功能结构域，一个是由338个氨基酸组成的先前未鉴定的结构域，另一个是由198个氨基酸组成的第二个结构域，该结构域与被鉴定为AK5的蛋白相对应，现在称为AK5p2。第一个结构域AK5p1，与AK5p2类似，以ATP或GTP作为磷酸供体，使AMP、CMP、dAMP和dCMP磷酸化。我们的数据表明，人类AK5有两个独立的功能结构域，且都具有酶活性。
