Immunochemical and catalytic characteristics of adenosine kinase from Leishmania donovani.
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF SHORT ISOFORM
Structure of human adenosine kinase at 1.5 A resolution.
Characterization and molecular cloning of an adenosine kinase from Babesia canis rossi.
Toxoplasma gondii adenosine kinase: expression, purification, characterization, crystallization and preliminary crystallographic analysis.
Structure-activity studies on mammalian adenosine kinase.
Design of adenosine kinase inhibitors from the NMR-based screening of fragments.
Adenosine kinase inhibitors. 2. Synthesis, enzyme inhibition, and antiseizure activity of diaryltubercidin analogues.
Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.
Crystal structure of adenosine kinase from Toxoplasma gondii at 1.8 A resolution.
Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon.
A single-domain cyclophilin from Leishmania donovani reactivates soluble aggregates of adenosine kinase by isomerase-independent chaperone function.
Design, synthesis, and structure-activity relationship of 6-alkynylpyrimidines as potent adenosine kinase inhibitors.
According to the literature [2], [5], & [10], the catalytic reaction of this enzyme proceeds via SN2-mechanism, in which acceptor 5'-hydroxyl group activated by a general base makes a nucleophilic attack on gamma-phosphate of ATP. Here, Asp318 (PDB;1dgy) acts as the general base. Moreover, Arg136 (PDB;1dgy) stabilizes the negatively charged gamma-phosphate group during transition state, together with an anion hole composed of mainchain amide of Gly315 and Gly317. These positive charged elements will increase the electrophilicity of the gamma-phosphate. Furthermore, magnesium ion plays an important role in the catalysis. However, whilst the ion is bridging beta- and gamma-phosphate groups of ATP in the enzyme from human, the magnesium ion interacts with alpha- and beta-phosphate groups in the enzyme from T. gondii. In either case, the magnesium ion would neutralize the negatively charged phosphate groups to facilitate the catalysis (see [10]).