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

被引:54
作者
Qin, Hui-Min [1 ,2 ]
Miyakawa, Takuya [1 ]
Inoue, Akira [3 ]
Nishiyama, Ryuji [3 ]
Nakamura, Akira [1 ]
Asano, Atsuko [1 ]
Ojima, Takao [3 ]
Tanokura, Masaru [1 ,2 ]
机构
[1] Univ Tokyo, Lab Basic Sci Hlth Longev, Dept Appl Biol Chem, Grad Sch Agr & Life Sci,Bunkyo Ku, 1-1-1 Yayoi, Tokyo 1138657, Japan
[2] Tianjin Univ Sci & Technol, Coll Biotechnol, 29,13th Ave, Tianjin 300457, Peoples R China
[3] Hokkaido Univ, Lab Marine Biotechnol & Microbiol, Grad Sch Fisheries Sci, 3-1-1 Minato Cho, Hakodate, Hokkaido 0418611, Japan
基金
中国国家自然科学基金;
关键词
SUBSTRATE RECOGNITION; MAJOR SOURCES; A1;
D O I
10.1039/c7cc06523j
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:555 / 558
页数:4
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