Eine Plattform für die Wissenschaft: Bauingenieurwesen, Architektur und Urbanistik
Eine Plattform für die Wissenschaft: Bauingenieurwesen, Architektur und Urbanistik
Structural Insight into the Catalytic Mechanisms of an L‐Sorbosone Dehydrogenase
L‐Sorbosone dehydrogenase (SNDH) is a key enzyme involved in the biosynthesis of 2‐keto‐L‐gulonic acid , which is a direct precursor for the industrial scale production of vitamin C. Elucidating the structure and the catalytic mechanism is essential for improving SNDH performance. By solving the crystal structures of SNDH from Gluconobacter oxydans WSH‐004, a reversible disulfide bond between Cys295 and the catalytic Cys296 residues is discovered. It allowed SNDH to switch between oxidation and reduction states, resulting in opening or closing the substrate pocket. Moreover, the Cys296 is found to affect the NADP+ binding pose with SNDH. Combining the in vitro biochemical and site‐directed mutagenesis studies, the redox‐based dynamic regulation and the catalytic mechanisms of SNDH are proposed. Moreover, the mutants with enhanced activity are obtained by extending substrate channels. This study not only elucidates the physiological control mechanism of the dehydrogenase, but also provides a theoretical basis for engineering similar enzymes.
Structural Insight into the Catalytic Mechanisms of an L‐Sorbosone Dehydrogenase
L‐Sorbosone dehydrogenase (SNDH) is a key enzyme involved in the biosynthesis of 2‐keto‐L‐gulonic acid , which is a direct precursor for the industrial scale production of vitamin C. Elucidating the structure and the catalytic mechanism is essential for improving SNDH performance. By solving the crystal structures of SNDH from Gluconobacter oxydans WSH‐004, a reversible disulfide bond between Cys295 and the catalytic Cys296 residues is discovered. It allowed SNDH to switch between oxidation and reduction states, resulting in opening or closing the substrate pocket. Moreover, the Cys296 is found to affect the NADP+ binding pose with SNDH. Combining the in vitro biochemical and site‐directed mutagenesis studies, the redox‐based dynamic regulation and the catalytic mechanisms of SNDH are proposed. Moreover, the mutants with enhanced activity are obtained by extending substrate channels. This study not only elucidates the physiological control mechanism of the dehydrogenase, but also provides a theoretical basis for engineering similar enzymes.
Structural Insight into the Catalytic Mechanisms of an L‐Sorbosone Dehydrogenase
Li, Dong (Autor:in) / Deng, Zhiwei (Autor:in) / Hou, Xiaodong (Autor:in) / Qin, Zhijie (Autor:in) / Wang, Xinglong (Autor:in) / Yin, Dejing (Autor:in) / Chen, Yue (Autor:in) / Rao, Yijian (Autor:in) / Chen, Jian (Autor:in) / Zhou, Jingwen (Autor:in)
Advanced Science ; 10
01.10.2023
15 pages
Aufsatz (Zeitschrift)
Elektronische Ressource
Englisch
Simulation insight into water transport mechanisms through multilayer graphene-based membrane
| British Library Online Contents | 2017
| American Chemical Society | 2021
Insight into catalytic effects of alkali metal salts addition on bamboo and cellulose pyrolysis
| Springer Verlag | 2024
Insight into catalytic effects of alkali metal salts addition on bamboo and cellulose pyrolysis
| DOAJ | 2024
Developing an insight into the particle-scale mechanisms that underlie suffusion in granular filters
| British Library Conference Proceedings | 2010