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    Home > Food News > Food Articles > Chinese scientists have revealed for the first time the crystal structure of a key enzyme in the synthesis of yeloroster

    Chinese scientists have revealed for the first time the crystal structure of a key enzyme in the synthesis of yeloroster

    • Last Update: 2021-02-28
    • Source: Internet
    • Author: User
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    Science and Technology Daily Beijing, October 30 (Reporter Ma Ailing) 30, the reporter was informed that the China Agriculture
    Biotechnology Research Institute, led by Dr. Cheng Qi, led the team for the first time revealed the key enzyme of photogenic biosynthesis - photodegenic primary folien oxidase 3D crystal structure, to understand how protein structure controls the catalytic action of important photodynamase has made a major breakthrough. The results were published recently in the scientific journal Nature.
    "everything grows by the sun", light-dependent primary pyroteinate oxidase is very important for the growth and development of green plants. Although it has been nearly 100 years since the discovery of this key enzyme, scientists have not been able to solve the mystery of its protein structure. In collaboration with Nigel Scruton Ph.D., Ph.D., Institute of Biotechnology, University of Manchester, UK, the
    Chengqi Task Force and Dr. Zhou Aiwu of shanghai Jiaoxuan University's School of Basic Medicine found the crystal structure of photo-dependent protophylogenic acid oxidase-nicotinamide dinucleotide phosphate protein complex. The clarification of crystal structure and the precise modeling of its ternate complex reveal how the relevant active bits carry out local hydrogenation transfer and long-distance proton transfer along the structure-defined proton transfer path, which promotes the reduction of photo-driven procyclics.
    " study provides a key missing link between the protein structure of the enzyme and excitation state chemistry, and is of great significance to the engineering design of photocatalytic chemical and biocatalysts and related protein small molecule inhibitors. Cheng Qi, co-author of the study, said the work also paves the way for detailed computational analysis of quantitative light-to-chemical energy conversion reactions, and a more complete description of the catalytic effect is a major challenge for enzymatics today.
    The study will help further improve the evolutionary sequence and future predictability of some key enzyme proteins in the process of convergence and evolution, said Sun Wenli, Ph.D., co-lead author of the study and Ph.D., China Agricultural
    Biotechnology Research Institute.
    it is known that the results have filled the gap in the three-dimensional crystal structure of photogenic chloroelogen biosynthetic photodynaminase and its cofactor complex in the world for nearly 100 years, which is of landmark significance.
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