Isolation and substrate specificity of an adenine nucleoside phosphorylase from adult Schistosoma mansoni
| Autor: | Todd M. Savarese, Mahmoud H. el Kouni |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
chemistry.chemical_classification
Adenine Purine nucleoside phosphorylase Adenine nucleoside Schistosoma mansoni Biology biology.organism_classification Molecular biology Adenosine Article Substrate Specificity chemistry.chemical_compound Glycogen phosphorylase Aglycone Enzyme chemistry Biochemistry medicine Animals Parasitology Pentosyltransferases Molecular Biology Phosphorolysis medicine.drug |
| Zdroj: | Molecular and biochemical parasitology. 194(1-2) |
| ISSN: | 1872-9428 |
| Popis: | 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 analogues 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. |
| Databáze: | OpenAIRE |
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