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

Chem Commun (Camb). 2018 Jan 11;54(5):555-558. doi: 10.1039/c7cc06523j.

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.

MeSH terms

  • Alginates / chemistry
  • Alginates / metabolism*
  • Flavobacterium / enzymology
  • Glucuronic Acid / chemistry
  • Glucuronic Acid / metabolism
  • Hexuronic Acids / chemistry
  • Hexuronic Acids / metabolism
  • Hydrogen-Ion Concentration
  • Models, Molecular
  • Molecular Structure
  • Polysaccharide-Lyases / chemistry
  • Polysaccharide-Lyases / genetics
  • Polysaccharide-Lyases / metabolism*

Substances

  • Alginates
  • Hexuronic Acids
  • Glucuronic Acid
  • Polysaccharide-Lyases
  • poly(beta-D-mannuronate) lyase