Enzymatic synthesis of 2'-ara and 2'-deoxy analogues of c-di-GMP
| Autor: | Anatoly I. Zinchenko, Alexander N. Rymko, Polina Shabunya, Anastasia S. Shchokolova, Svetlana A. Fatykhava, Sergey V. Kvach |
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| Rok vydání: | 2015 |
| Předmět: |
GTP'
Stereochemistry Deoxyguanosine monophosphate Allosteric regulation Biochemistry Inclusion bodies law.invention chemistry.chemical_compound Bacterial Proteins law Genetics Thermotoga maritima Cyclic GMP chemistry.chemical_classification biology Arabinonucleotides Escherichia coli Proteins Deoxyguanine Nucleotides General Medicine biology.organism_classification Enzyme chemistry Recombinant DNA biology.protein bacteria Molecular Medicine Diguanylate cyclase Guanosine Triphosphate Phosphorus-Oxygen Lyases |
| Zdroj: | Nucleosides, nucleotidesnucleic acids. 34(6) |
| ISSN: | 1532-2335 |
| Popis: | The substrate specificity of recombinant full-length diguanylate cyclase (DGC) of Thermotoga maritima with mutant allosteric site was investigated. It has been originally shown that the enzyme could use GTP closest analogues – 2′-deoxyguanosine-5′-triphosphate (dGTP) and 9-β-D-arabinofuranosyl-guanine-5′-triphosphate (araGTP) as the substrates. The first demonstrations of an enzymatic synthesis of bis-(3′-5′)-cyclic dimeric deoxyguanosine monophosphate (c-di-dGMP) and the previously unknown bis-(3′-5′)-cyclic dimeric araguanosine monophosphate (c-di-araGMP) using DGC of T. maritima in the form of inclusion bodies have been provided. |
| Databáze: | OpenAIRE |
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