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

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Abstract

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 Mr 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. © 1995.

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Strong, S. J., & Ellington, W. R. (1995). Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 1246(2), 197–200. https://doi.org/10.1016/0167-4838(94)00218-6

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