Reaction kinetics and inhibition of adenosine kinase from Leishmania donovani
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Cited by (22)
Concentration of 2C-methyladenosine triphosphate by Leishmania guyanensis enables specific inhibition of Leishmania RNA virus 1 via its RNA polymerase
2018, Journal of Biological ChemistryCitation Excerpt :This likely reflects the fact that as purine auxotrophs, Leishmania parasites must avidly scavenge all naturally occurring purines from their environment, through a combination of powerful transporters and metabolic interconversions (32). One particularly important step for 2CMA and related inhibitors may be adenosine kinase (47, 48), which may mediate the initial and often rate-limiting phosphorylation of antiviral nucleosides (44, 49). Strong accumulation of toxic anti-leishmanial purines has also been noted in earlier studies (50, 51).
Potential chemotherapeutic targets in the purine metabolism of parasites
2003, Pharmacology and TherapeuticsCrystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism prodrug binding
2000, Journal of Molecular BiologyCitation Excerpt :However, beyond this ribose-induced closure of its small and large domains, only small tertiary structural changes are found among the apo, ribose and ribose:ADP-bound enzyme forms, and many aspects of its catalytic mechanism are still unclear (Sigrell et al., 1999). Similarly, the structure of the human AK:adenosine complex, although providing some insight into substrate binding, left many questions about its catalytic mechanism unanswered; the pertinent biochemical data regarding the enzymatic mechanism are equivocal and controversial, and thus, this structure could not resolve all issues (Henderson et al., 1972; Palella et al., 1980; Rotllan et al., 1985; Hawkins et al., 1987; Bhaumik et al., 1988). In order to understand better the structural and mechanistic basis for phosphate transfer by this class of carbohydrate kinases, we determined the structures of the T. gondii apo AK to 2.55 Å resolution, the AK:adenosine complex to 2.50 Å resolution, and the AK:adenosine:AMP-PCP (a non-hydrolysable ATP analog) ternary complex to 1.71 Å resolution.
Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding
2000, Journal of Molecular BiologyCitation Excerpt :However, beyond this ribose-induced closure of its small and large domains, only small tertiary structural changes are found among the apo, ribose and ribose:ADP-bound enzyme forms, and many aspects of its catalytic mechanism are still unclear (Sigrell et al., 1999). Similarly, the structure of the human AK:adenosine complex, although providing some insight into substrate binding, left many questions about its catalytic mechanism unanswered; the pertinent biochemical data regarding the enzymatic mechanism are equivocal and controversial, and thus, this structure could not resolve all issues (Henderson et al., 1972; Palella et al., 1980; Rotllan et al., 1985; Hawkins et al., 1987; Bhaumik et al., 1988). In order to understand better the structural and mechanistic basis for phosphate transfer by this class of carbohydrate kinases, we determined the structures of the T. gondii apo AK to 2.55 Å resolution, the AK:adenosine complex to 2.50 Å resolution, and the AK:adenosine:AMP-PCP (a non-hydrolysable ATP analog) ternary complex to 1.71 Å resolution.
Production of adenosine and nucleoside analogs by the exchange reaction catalyzed by rat liver adenosine kinase
1995, Biochemical PharmacologyActive site thiol(s) in Leishmania donovani adenosine kinase: comparison with hamster enzyme and evidence for the absence of regulatory adenosine binding site
1992, Molecular and Biochemical Parasitology