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• W2000480344 abstract "Adenosine kinase (AK) is a key enzyme in the regulation of extracellular adenosine and intracellular adenylate levels. Inhibitors of adenosine kinase elevate adenosine to levels that activate nearby adenosine receptors and produce a wide variety of therapeutically beneficial activities. Accordingly, AK is a promising target for new analgesic, neuroprotective, and cardioprotective agents. We determined the structure of human adenosine kinase by X-ray crystallography using MAD phasing techniques and refined the structure to 1.5 Å resolution. The enzyme structure consisted of one large α/β domain with nine β-strands, eight α-helices, and one small α/β-domain with five β-strands and two α-helices. The active site is formed along the edge of the β-sheet in the large domain while the small domain acts as a lid to cover the upper face of the active site. The overall structure is similar to the recently reported structure of ribokinase from Escherichia coli [Sigrell et al. (1998) Structure 6, 183−193]. The structure of ribokinase was determined at 1.8 Å resolution and represents the first structure of a new family of carbohydrate kinases. Two molecules of adenosine were present in the AK crystal structure with one adenosine molecule located in a site that matches the ribose site in ribokinase and probably represents the substrate-binding site. The second adenosine site overlaps the ADP site in ribokinase and probably represents the ATP site. A Mg2+ ion binding site is observed in a trough between the two adenosine sites. The structure of the active site is consistent with the observed substrate specificity. The active-site model suggests that Asp300 is an important catalytic residue involved in the deprotonation of the 5‘-hydroxyl during the phosphate transfer." @default.
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• W2000480344 date "1998-10-22" @default.
• W2000480344 modified "2023-10-10" @default.
• W2000480344 title "Structure of Human Adenosine Kinase at 1.5 Å Resolution^," @default.
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• W2000480344 doi "https://doi.org/10.1021/bi9815445" @default.
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