Arginine kinase shows nucleoside diphosphate kinase-like activity toward deoxythymidine diphosphate

Alonso A. Lopez-Zavala, Rogerio R. Sotelo-Mundo, Jose M. Hernandez-Flores, Maria E. Lugo-Sanchez, Rocio Sugich-Miranda, Karina D. Garcia-Orozco

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

4 Citas (Scopus)


© 2016, Springer Science+Business Media New York. Arginine kinase (AK) (ATP: L-arginine phosphotransferase, E.C. catalyzes the reversible transfer of ATP γ-phosphate group to L-arginine to synthetize phospho-arginine as a high-energy storage. Previous studies suggest additional roles for AK in cellular processes. Since AK is found only in invertebrates and it is homologous to creatine kinase from vertebrates, the objective of this work was to demonstrate nucleoside diphosphate kinase-like activity for shrimp AK. For this, AK from marine shrimp Litopenaeus vannamei (LvAK) was purified and its activity was assayed for phosphorylation of TDP using ATP as phosphate donor. Moreover, by using high-pressure liquid chromatography (HPLC) the phosphate transfer reaction was followed. Also, LvAK tryptophan fluorescence emission changes were detected by dTDP titration, suggesting that the hydrophobic environment of Trp 221, which is located in the top of the active site, is perturbed upon dTDP binding. The kinetic constants for both substrates Arg and dTDP were calculated by isothermal titration calorimetry (ITC). Besides, docking calculations suggested that dTDP could bind LvAK in the same cavity where ATP bind, and LvAK basic residues (Arg124, 126 and 309) stabilize the dTDP phosphate groups and the pyrimidine base interact with His284 and Ser122. These results suggest that LvAK bind and phosphorylate dTDP being ATP the phosphate donor, thus describing a novel alternate nucleoside diphosphate kinase-like activity for this enzyme.
Idioma originalInglés estadounidense
Páginas (desde-hasta)301-308
Número de páginas8
PublicaciónJournal of Bioenergetics and Biomembranes
EstadoPublicada - 1 jun 2016


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