Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues

• Published in: Biochimica et biophysica acta 1995-01, Vol.1246 (2), p.197-200
• Main Authors: Strong, Scott J., Ellington, W.Ross
• Format: Article
• Language: English
• Subjects: Active site residue; Amino Acid Sequence; Animals; Arginine kinase; Arginine Kinase - genetics; Base Sequence; Binding Sites; Catalysis; Cloning, Molecular; Creatine kinase; DNA, Complementary - chemistry; Horseshoe Crabs - genetics; Molecular Sequence Data; Phosphagen kinase
• ISSN: 0167-4838; 0006-3002; 1879-2588
• DOI: 10.1016/0167-4838(94)00218-6

The gene for arginine kinase (AK; EC 2.7.3.3) from the horseshoe crab, Limulus polyphemus, was cloned and the complete cDNA sequence was determined. An open reading frame with 1071 nucleotides was detected that encodes a 357 amino-acid protein with a calculated M r of 40 238. The coding transcript is flanked by 13 and 512 nucleotides of 5′ and 3′ untranslated regions, respectively. The deduced amino-acid sequence of Limulus AK displays extensive similarity to other arginine kinases, vertebrate and invertebrate creatine kinases (CK) and a glycocyamine kinase (GK). Consensus AK and consensus CK sequences, as well as a GK sequence, were compared to CK peptide regions containing residues presumed to be important in catalysis and/or located in close proximity to the active site. Our comparisons revealed some inconsistencies with hypothesized roles of particular residues in catalytic function.