119240-26-5Relevant articles and documents
Reversible and in Situ Formation of Organic Arsenates and Vanadates as Organic Phosphate Mimics in Enzymatic Reactions: Mechanistic Investigation of Aldol Reactions and Synthetic Applications
Drueckhammer, Dale G.,Durrwachter, J. Robert,Pederson, Richard L.,Crans, Debbie C.,Daniels, Lacy,Wong, Chi-Huey
, p. 70 - 77 (1989)
A synthetic strategy is developed that uses organic phosphate utilizing enzymes as catalysts and a mixture of an organic alcohol and inorganic arsenate or vanadate to replace the organic phosphate substrate.In this process, inorganic arsenate or vanadate reacts with the alcohol reversibly in situ to form a mixture of esters, one of which is accepted by the enzyme as a substrate.Examples of the utility of this approach are demonstrated in enzymatic aldol condensations catalyzed by fructose-1,6-diphosphate aldolase, fuculose-1-phosphate aldolase, and rhamnulose-1-phosphate aldolase with a mixture of dihydroxyacetone and inorganic arsenate as substrate.Several uncommon sugars and deoxy sugars are prepared on 5-17-mmol scales.Mechanistic studies on an aldol reaction indicate that the redox reaction between dihydroxyacetone and inorganic vanadate prohibits the use of such a mixture to replace dihydroxyacetone phosphate in enzymatic aldol condensations.
Characterization of pyrimidine nucleoside phosphorylase of Mycoplasma hyorhinis: Implications for the clinical efficacy of nucleoside analogues
Vande Voorde, Johan,Gago, Federico,Vrancken, Kristof,Liekens, Sandra,Balzarini, Jan
experimental part, p. 113 - 123 (2012/10/23)
In the present paper we demonstrate that the cytostatic and antiviral activity of pyrimidine nucleoside analogues is markedly decreased by a Mycoplasma hyorhinis infection and show that the phosphorolytic activity of the mycoplasmas is responsible for this. Since mycoplasmas are (i) an important cause of secondary infections in immunocompromised (e.g. HIV infected) patients and (ii) known to preferentially colonize tumour tissue in cancer patients, catabolic mycoplasma enzymesmay compromise efficient chemotherapy of virus infections and cancer. In the genome of M. hyorhinis, a TP (thymidine phosphorylase) gene has been annotated. This gene was cloned, expressed in Escherichia coli and kinetically characterized. Whereas the mycoplasma TP efficiently catalyses the phosphorolysis of thymidine (Km = 473 μM) and deoxyuridine (Km = 578 μM), it prefers uridine (K m =92 μM) as a substrate. Our kinetic data and sequence analysis revealed that the annotated M. hyorhinis TP belongs to the NP (nucleoside phosphorylase)-II class PyNPs (pyrimidine NPs), and is distinct from the NP-II class TP and NPI class UPs (uridine phosphorylases). M. hyorhinis PyNP also markedly differs from TP and UP in its substrate specificity towards therapeutic nucleoside analogues and susceptibility to clinically relevant drugs. Several kinetic properties of mycoplasma PyNP were explained by in silico analyses. The Authors Journal compilation
