Issue 5, 2018

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

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.

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

Supplementary files

Article information

Article type
Communication
Submitted
19 Aug 2017
Accepted
26 Oct 2017
First published
02 Jan 2018
This article is Open Access
Creative Commons BY-NC license

Chem. Commun., 2018,54, 555-558

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

H. Qin, T. Miyakawa, A. Inoue, R. Nishiyama, A. Nakamura, A. Asano, T. Ojima and M. Tanokura, Chem. Commun., 2018, 54, 555 DOI: 10.1039/C7CC06523J

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