Structural basis for controlling the enzymatic properties of polymannuronate preferred alginate lyase FlAlyA from the PL-7 family. Issue 5 (2nd January 2018)

• Record Type: Journal Article
• Authors: Qin, Hui-Min; Miyakawa, Takuya; Inoue, Akira; Nishiyama, Ryuji; Nakamura, Akira; Asano, Atsuko; Ojima, Takao; Tanokura, Masaru
• Is Part Of: Chemical communications. Volume 54:Issue 5(2018)
• Page Start: 555
• Page End: 558
• Publication Date: 2018-01-02
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c7cc06523j
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Alginate-recognition subsites of alginate lyase FlAlyA were characterized as potential targets for engineering alginate oligosaccharides that are useful biomaterials. 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.