Characterization Of An Atypical, Thermostable, Organic Solvent- And Acid-Tolerant 2′-Deoxyribosyltransferase From Chroococcidiopsis Thermalis
In our search for thermophilic and acid-tolerant nucleoside 2′-deoxyribosyltransferases (NDTs), we found a good candidate in an enzyme encoded by Chroococcidiopsis thermalis PCC 7203 (CtNDT). Biophysical and biochemical characterization revealed CtNDT as a homotetramer endowed with good activity and...
| Autores: | , , , , |
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| Formato: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2018 |
| País: | Colombia |
| Recursos: | Corporación Universidad de la Costa |
| Repositorio: | Repositorio REDICUC |
| Idioma: | inglés |
| OAI Identifier: | oai:repositorio.cuc.edu.co:11323/1093 |
| Acesso em linha: | https://hdl.handle.net/11323/1093 https://repositorio.cuc.edu.co/ |
| Access Level: | acceso abierto |
| Palavra-chave: | Enzymatic Synthesis Extremophiles Homology Modeling Nucleoside 2′-Deoxyribosyltransferase Nucleoside Analogues |
| Resumo: | In our search for thermophilic and acid-tolerant nucleoside 2′-deoxyribosyltransferases (NDTs), we found a good candidate in an enzyme encoded by Chroococcidiopsis thermalis PCC 7203 (CtNDT). Biophysical and biochemical characterization revealed CtNDT as a homotetramer endowed with good activity and stability at both high temperatures (50–100 °C) and a wide range of pH values (from 3 to 7). CtNDT recognizes purine bases and their corresponding 2′-deoxynucleosides but is also proficient using cytosine and 2′-deoxycytidine as substrates. These unusual features preclude the strict classification of CtNDT as either a type I or a type II NDT and further suggest that this simple subdivision may need to be updated in the future. Our findings also hint at a possible link between oligomeric state and NDT’s substrate specificity. Interestingly from a practical perspective, CtNDT displays high activity (80–100%) in the presence of several water-miscible co-solvents in a proportion of up to 20% and was successfully employed in the enzymatic production of several therapeutic nucleosides such as didanosine, vidarabine, and cytarabine. |
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