Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle.

Arginine kinase belongs to an evolutionary conserved family of ATP:guanidino phosphotransferases, whose members play an important role in energy metabolism. In this work, a lambda gt11 lobster muscle library was constructed and screened by using both polyclonal antibodies and two synthetic oligonucleotides. The complete amino acid sequence of arginine kinase (ATP:L-arginine N-phosphotransferase, EC 2.7.3.3) from lobster muscle was determined by cloning and sequencing the DNA complementary to its mRNA. The identity of the clone was confirmed by comparing the amino acid sequence deduced by nucleotide sequence analysis with previously published partial sequences of amino- and carboxyl-terminal regions of the enzyme and some of its fragments (Regnouf, F., Kassab, R., Debuire, B., Richard, C., and Han K. K. (1981) Int. J. Peptide Protein Res. 17, 143-155). The nucleotide sequence of the cDNA was found to contain an open reading frame encoding 355 amino acid residues with a calculated molecular mass of 39,830 daltons. This enzyme exhibits a significant sequence identity to those of representative members of the guanidino kinase family, including creatine kinase. This report represents the first molecular cloning and sequencing of an ATP-guanidino phosphotransferase which is not a creatine kinase isoform.