Arginine kinase (AK, EC 2.7.3.3) plays an important role in cells with high, fluctuating energy requirements. In invertebrates, AK is the major phosphagen kinase that modulates the energy metabolism. Here, the full-length cDNA sequence encoding arginine kinase (EcAK) was obtained from the Exopalaemon carinicauda. The complete nucleotide sequence of EcAK contained a 1068 bp open reading frame (ORF) encoding EcAK precursor of 355 amino acids. The genomic DNA fragment of EcAK with the corresponding cDNA sequence is composed of 4 exons and 3 introns. The domain architecture of the deduced EcAK protein contained an ATP-gua_PtransN domain and an ATP-gua_Ptrans domain. EcAK mRNA was predominantly expressed in the muscle. The expression of EcAK in the prawns challenged with Vibrio parahaemolyticus and Aeromonas hydrophila changed in a time-dependent manner. Then, EcAK was recombinantly expressed in Pichia pastoris and the purified recombinant EcAK had the same enzymatic characterization as AK from the muscle of Euphausia superba. In conclusion, EcAK may play the same biological activity in E. carinicauda as those from other crustaceans.

精氨酸激酶（AK，EC 2.7.3.3）在能量需求高且波动的细胞中起重要作用。在无脊椎动物中，AK是调节能量代谢的主要磷酸酶激酶。在此，从Exopalaemon carinicauda获得了编码精氨酸激酶（EcAK）的全长cDNA序列。EcAK的完整核苷酸序列包含一个1068 bp的开放阅读框（ORF），编码355个氨基酸的EcAK前体。具有相应cDNA序列的EcAK的基因组DNA片段由4个外显子和3个内含子组成。推导的EcAK蛋白的结构域结构包含一个ATP-gua_PtransN结构域和一个ATP-gua_Ptrans结构域。EcAKmRNA主要在肌肉中表达。副溶血弧菌和嗜水气单胞菌攻击的虾中EcAK的表达随时间变化。然后，EcAK在巴斯德毕赤酵母中重组表达，并且纯化的重组EcAK具有与来自Euphausia superba的肌肉的AK相同的酶学特征。总之，EcAK在大肠杆菌中可能与其他甲壳类动物具有相同的生物活性。