Trypanosoma cruzi Arginine Kinase Characterization and Cloning

Abstract

N-Phosphorylated guanidino compounds, commonly referred to as phosphagens, play a critical role as an energy reserve because of the high energy phosphate that can be transferred when the renewal of ATP is needed. It has also been proposed that these compounds function in spatial buffering of cellular energy production sites. So, phosphagens act as reserves not only of ATP but also of inorganic phosphate, which is mostly returned to the medium by metabolic consumption of ATP. Phosphoarginine is the main reserve of high energy phosphate compounds in a wide variety of invertebrates. In addition phosphocreatine, phosphoglycocyamine, phosphotaurocyamine, phosphohypotaurocyamine, phosphoopheline, and phospholombricine are also found, whereas in vertebrates the only one present is phosphocreatine (1, 2).Arginine kinase (EC 2.7.3.3) is a member of a conserved family of phosphotransferases which also includes creatine kinase. These enzymes catalyze the reversible transfer of a phosphoryl group from ATP to a guanidino acceptor, which can be either an amino acid (e.g. lombricine or arginine) or a carboxylate (e.g. creatine or glycocyamine; Reaction 1).

Proteomics and Immunological Analysis of a Novel Shrimp Allergen, Pen m 2

“…The active site residue of Pen m 2 was recognized by sequence comparison as Cys 271 . The guanidino specificity region, suggested to be generally conserved in most arginine kinase sequences and with 16 residues (residues Ser 56 to Asp 71 ) highly conserved in crustaceans and associated with substrate binding (37), was also found in Pen m 2, as was a putative actinin type actin-binding domain (residues Asp 214 to Asn 223 ) (38).…”

Two-domain arginine kinase from the deep-sea clam Calyptogena kaikoi—Evidence of two active domains

“…Members of this enzyme family play a key role in animals as ATP buffering systems in cells that display high and variable rates of ATP turnover [Kenyon and Reed, 1983;Wyss et al, 1992;Ellington, 2001]. AK is most widely distributed among organisms; its activity has been observed in arthropods, molluscs, nematoda, cnidarians, poriferae (the most ancient multi-cellular organisms), protozoans (ciliates, Trypanosoma and choanoflagellates) and bacteria [Watts and Bannister, 1970;Noguchi et al, 2001;Pereira et al, 2000;Uda et al, 2006;Conejo et al, 2008;Andrews et al, 2008], indicating an ancient origin of AK. Most AKs are monomers with a relative molecular mass of approximately 40 kDa [Morrison, 1973].…”

Functional Expression of Phosphagen Kinase Systems Confers Resistance to Transient Stresses in Saccharomyces cerevisiae by Buffering the ATP Pool

“…The common feature of these kinases is their capability to synthesize a metabolically inert pool of phosphorylated compounds (phosphagens) during normal metabolic conditions and to replenish the ATP from this pool during periods of high energetic demand. Eight phosphagen kinases are found in the animal kingdom (3), with arginine kinase (AK; EC 2.7.3.3) as a prominent example, occurring in insects (4), crustaceans (5), and in certain unicellular organisms (6). In analogy to CK, AK catalyzes the following reaction: MgADP Ϫ ϩ PArg 2Ϫ ϩ H ϩ i MgATP 2Ϫ ϩ Arg.…”

“…Although microorganisms are often exposed to rapidly changing environmental conditions and fluctuating availability of energy, phosphagen kinase systems occur only in few unicellular organisms, e.g. Paramecium caudatum and Trypanosoma cruzi (6,11). Thus, we hypothesized that lower unicellular eukaryotes, such as the yeast Saccharomyces cerevisiae, would potentially benefit if artificially equipped with such phosphagen kinase systems.…”