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Isolation and substrate specificity of an adenine nucleoside phosphorylase from adult Schistosoma mansoni. | LitMetric

Isolation and substrate specificity of an adenine nucleoside phosphorylase from adult Schistosoma mansoni.

Mol Biochem Parasitol

Division of Biology and Medicine, Brown University, RI 02912, USA; Department of Pharmacology and Toxicology, University of Alabama at Birmingham, Birmingham, AL 35294, USA. Electronic address:

Published: January 2015

An adenine nucleoside phosphorylase (ANP, EC none) activity was identified and partially purified from extracts of Schistosoma mansoni by chromatofocussing column chromatography and molecular sieving. The enzyme is distinct from purine nucleoside phosphorylase (PNP, EC 2.4.2.1). ANP is specific for adenine nucleosides which includes adenosine analogs modified in the aglycone, pentose or both moieties. (e.g. 2'-deoxyadenosine, 5'-deoxy-5'-methylthioadenosine, 5'-deoxy-5'-iodo-2-fluoroadenosine, etc.) The enzyme is also distinct from the mammalian 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28) in that it is able of the phosphorolysis of 2'-deoxyadenosine while mammalian MTAP cannot. Because of ANP unique substrate specificity, the enzyme could play a role as a target for chemotherapy of these parasites. Cytotoxic analogs may be designed as subversive substrates that are selectively activated only by the schistosomal ANP.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4073610PMC
http://dx.doi.org/10.1016/j.molbiopara.2014.04.008DOI Listing

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