控制来自PL-7家族的聚甘露糖醛酸偏好性海藻酸裂解酶FlAlyA酶学性质的结构基础。
Structural basis for controlling the enzymatic properties of polymannuronate preferred alginate lyase FlAlyA from the PL-7 family.
作者信息
Qin Hui-Min, Miyakawa Takuya, Inoue Akira, Nishiyama Ryuji, Nakamura Akira, Asano Atsuko, Ojima Takao, Tanokura Masaru
机构信息
Laboratory of Basic Science on Healthy Longevity, Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo, Tokyo 113-8657, Japan.
出版信息
Chem Commun (Camb). 2018 Jan 11;54(5):555-558. doi: 10.1039/c7cc06523j.
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.
FlAlyA是一种偏好聚甘露糖醛酸的内切酶。晶体结构和诱变研究表明，外部糖醛酸结合亚位点+2、+3和-2处的结构变化控制着PL-7家族酶的酶学性质。赖氨酸158突变改变了pH依赖性并提高了单糖和二糖的产量。
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