carba Nicotinamide Adenine Dinucleotide Phosphate: Robust Cofactor for Redox Biocatalysis

被引：19

作者：

Zachos, Ioannis ^{[1
]}

Doering, Manuel ^{[1
,2
]}

Tafertshofer, Georg ^{[3
]}

Simon, Robert C. ^{[3
]}

Sieber, Volker ^{[1
,2
,4
,5
]}

机构：

[1] Tech Univ Munich, Chair Chem Biogen Resources, Campus Straubing Biotechnol & Sustainabil, Schulgasse 16, D-94315 Straubing, Germany

[2] Tech Univ Munich, Synbiofoundry TUM, Schulgasse 16, D-94315 Straubing, Germany

[3] Roche Diagnost GmbH, DOZCBE 6164, Nonnenwald 2, D-82377 Penzberg, Germany

[4] Tech Univ Munich, Catalyt Res Ctr, Ernst Otto Fischer Str 1, D-85748 Garching, Germany

[5] Univ Queensland, Sch Chem & Mol Biosci, 68 Copper Rd, St Lucia, Qld 4072, Australia

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2021年 / 60卷 / 26期

关键词：

biocatalysis; biomimic; cNADP; oxidoreductases; regeneration system;

D O I：

10.1002/anie.202017027

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：14701 / 14706

页数：6

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