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Updated: Feb 16, 2026

Alginate Hydrogels for Three-Dimensional Organ Culture of Ovaries and Oviducts
Published on: June 20, 2011
Structural basis for controlling the enzymatic properties of polymannuronate preferred alginate lyase FlAlyA from the
Hui-Min Qin1, Takuya Miyakawa, Akira Inoue
1Laboratory 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. amtanok@mail.ecc.u-tokyo.ac.jp.
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.
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