Structural highlights
Publication Abstract from PubMed
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.
Structural basis for controlling the enzymatic properties of polymannuronate preferred alginate lyase FlAlyA from the PL-7 family.,Qin HM, Miyakawa T, Inoue A, Nishiyama R, Nakamura A, Asano A, Ojima T, Tanokura M Chem Commun (Camb). 2018 Jan 11;54(5):555-558. doi: 10.1039/c7cc06523j. PMID:29292806[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Qin HM, Miyakawa T, Inoue A, Nishiyama R, Nakamura A, Asano A, Ojima T, Tanokura M. 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. PMID:29292806 doi:http://dx.doi.org/10.1039/c7cc06523j
