carba Nicotinamide Adenine Dinucleotide Phosphate: Robust Cofactor for Redox Biocatalysis
| Autor: | Manuel Döring, Ioannis Zachos, Georg Tafertshofer, Robert C. Simon, Volker Sieber |
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| Rok vydání: | 2020 |
| Předmět: |
biomimic
Molecular Conformation 010402 general chemistry 01 natural sciences Redox Catalysis Cofactor regeneration system chemistry.chemical_compound Ribose Research Articles chemistry.chemical_classification biology Nicotinamide 010405 organic chemistry Temperature General Chemistry Phosphate Combinatorial chemistry 0104 chemical sciences ddc Enzyme chemistry Biocatalysis biology.protein cNADP Oxidoreductases Oxidation-Reduction Nicotinamide adenine dinucleotide phosphate NADP Research Article |
| Zdroj: | Angewandte Chemie (International Ed. in English) |
| Popis: | Here we report a new robust nicotinamide dinucleotide phosphate cofactor analog (carba‐NADP+) and its acceptance by many enzymes in the class of oxidoreductases. Replacing one ribose oxygen with a methylene group of the natural NADP+ was found to enhance stability dramatically. Decomposition experiments at moderate and high temperatures with the cofactors showed a drastic increase in half‐life time at elevated temperatures since it significantly disfavors hydrolysis of the pyridinium‐N−glycoside bond. Overall, more than 27 different oxidoreductases were successfully tested, and a thorough analytical characterization and comparison is given. The cofactor carba‐NADP+ opens up the field of redox‐biocatalysis under harsh conditions. A robust cofactor analog (carba‐NADP+) is described here with a 33‐times longer half‐life time when the cofactor is heated up to 50 °C. Decomposition experiments on the reduced form at low pH values showed a drastic increase in stability. The cofactor is found to make a significant contribution to the field of redox‐biocatalysis under harsh conditions retaining most of its enzymatic activity. |
| Databáze: | OpenAIRE |
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