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    Home > Biochemistry News > Biotechnology News > The design and modification of fatty acid lysase extends the product spectrum of fatty acid synthesis machines.

    The design and modification of fatty acid lysase extends the product spectrum of fatty acid synthesis machines.

    • Last Update: 2020-09-12
    • Source: Internet
    • Author: User
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    Recently, Zhao Zongbao, a researcher in the Biomass Efficient Conversion Research Group of the Biotechnology Department of the Dalian Institute of Chemical Physics of the Chinese Academy of Sciences, teamed up with Jens Nielsen, a professor at Chalmers University of Technology in Sweden, and Martin Grininger, a professor at the University of Frankfurt in Germany, to make new progress in the study of fungal fatty acid chelase modification: Design The results of the study, published in Nature Chemical Biology (DOI:10.1038/nchembio.2301) and published in the April issue of the cover story, have transformed fatty acid lysase and expanded the product spectrum of fatty acid synthesis machines.
    fatty acids are important molecules that make up cells and are the basic raw materials for biofuels and grease chemicals.
    fatty acid lysase (FAS) is the key enzyme for cell synthesis of fatty acids, while the FAS catalytic activity of fungal sources is relatively high.
    fungal FAS is a versatile enzyme with 7 different catalytic domains (AT, ER, DH, MPT, KR, KS and PPT) and 1 ayl-based carrier protein (ACP) domain with a molecular weight of approximately 2.7 million Daltons that can be assembled into caged supermolecular structures.
    the catalytic mechanisms and crystal structure of fungal FAS have been explained, it is often considered difficult to manipulate and adapt because of its complexity.
    The team's previous multi-histological study of oil-producing yeast found that the round red winter spore yeast carried a FAS containing two ayl-based carrier protein (ACP) domains (Nat.Commun.2012, 3,1112);
    recent study found that fatty acid synthesis can be performed with just one ACP.
    As a result, the researchers replaced one of the ACPs with a bacterial source of thioesterase (TE), resulting in hybrid FAS that mainly produces medium/short-chain-length fatty acids;
    the results show that embedding iso-origin proteins into the supermomeric structure of the fungus FAS cage can result in a new function of fatty acid synthesis machines, which can provide a new route for bioman making by borrowing fatty acid synthesis pathways.
    the above-mentioned research has been funded by the National Natural Science Foundation of China and assisted by the Research Group on New Materials and New Technologies for Biological Separation And Analysis of Dalian Chemical Institute and the Public Analysis and Testing Group.
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