carba Nicotinamide Adenine Dinucleotide Phosphate: Robust Cofactor for Redox Biocatalysis | Zendy

Zachos Ioannis | Zendy; Döring Manuel | Zendy; Tafertshofer Georg | Zendy; Simon Robert C. | Zendy; Sieber Volker | Zendy

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carba Nicotinamide Adenine Dinucleotide Phosphate: Robust Cofactor for Redox Biocatalysis

Author(s) -

Zachos Ioannis,

Döring Manuel,

Tafertshofer Georg,

Simon Robert C.,

Sieber Volker

Publication year - 2021

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.202017027

Subject(s) - cofactor , biocatalysis , nad+ kinase , nicotinamide adenine dinucleotide phosphate , nicotinamide adenine dinucleotide , chemistry , redox , niacinamide , nicotinamide , pyridinium , enzyme , stereochemistry , biochemistry , organic chemistry , reaction mechanism , catalysis , oxidase test

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.

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