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

• Published in: Journal of bioenergetics and biomembranes Vol. 48; no. 3; pp. 301 - 308
• Main Authors: Lopez-Zavala, Alonso A., Sotelo-Mundo, Rogerio R., Hernandez-Flores, Jose M., Lugo-Sanchez, Maria E., Sugich-Miranda, Rocio, Garcia-Orozco, Karina D.
• Format: Journal Article
• Language: English
• Published: New York Springer US 01.06.2016; Springer Nature B.V
• Subjects: Adenosine Triphosphate - metabolism; Animal Anatomy; Animal Biochemistry; Animals; Arginine Kinase - metabolism; ATP; Biochemistry; Bioorganic Chemistry; Calorimetry; Chemistry; Chemistry and Materials Science; Chromatography; Energy storage; Histology; Kinases; Liquid chromatography; Molecular Docking Simulation; Morphology; Nucleoside-Diphosphate Kinase - metabolism; Organic Chemistry; Penaeidae - enzymology; Phosphorylation; Shellfish; Studies; Thymine Nucleotides - metabolism; ITC; Tryptophan quenching; Docking; dTDP; Nucleoside diphosphate kinase; Arginine kinase; Litopenaeus vannamei

Arginine kinase (AK) (ATP: L-arginine phosphotransferase, E.C. 2.7.3.3) 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...