Structural basis for controlling the enzymatic properties of polymannuronate preferred alginate lyase FlAlyA from the PL-7 family

Chemical Communications : Chem Comm
Hui-Min QinMasaru Tanokura

Abstract

FlAlyA is an endolytic enzyme with a preference for polymannuronate. The crystal structure and mutagenesis studies elucidated that the structural variations at outer uronate-binding subsites +2, +3 and -2 control the enzymatic properties of PL-7 family enzymes. Lys158 mutations changed the pH dependency and enhanced the production of mono- and disaccharides.

References

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Oct 23, 2009·The Journal of Biological Chemistry·Kohei OguraKousaku Murata
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Dec 25, 2016·The Journal of Biological Chemistry·Hui-Min QinMasaru Tanokura

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Citations

Aug 6, 2019·International Journal of Biological Macromolecules·Benwei ZhuHeng Yin
Feb 6, 2020·International Journal of Biological Macromolecules·Xiaojun WuJunjie Li
Dec 19, 2020·Comprehensive Reviews in Food Science and Food Safety·Jun LiuZhengqiang Jiang
Mar 2, 2021·Acta Crystallographica. Section D, Structural Biology·Keke ZhangQianqian Lyu
Feb 23, 2021·International Journal of Biological Macromolecules·Chuhuan HuYapeng Fang
Aug 12, 2020·Current Drug Delivery·Dhalendra KothaleDharmendra Jain
Jun 5, 2018·Biochimica Et Biophysica Acta. General Subjects·Qianqian LyuWeizhi Liu
May 1, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Nadezhda ChernyshevaMarina Isaeva
Jul 20, 2021·Biotechnology for Biofuels·Lanzeng ZhangLushan Wang
Aug 29, 2020·Journal of Agricultural and Food Chemistry·Chao LiHui-Min Qin
Dec 13, 2018·ACS Chemical Neuroscience·Longgang JiaFufeng Liu
Jul 11, 2021·Glycobiology·Sébastien ViolotLionel Ballut
Sep 24, 2021·Journal of Agricultural and Food Chemistry·Xin GaoHui-Min Qin

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