Unraveling the subtleties of β-(1→3)-glucan phosphorylase specificity in the GH94, GH149, and GH161 glycoside hydrolase families.

The Journal of Biological Chemistry
Sakonwan KuhaudomlarpRobert A Field

Abstract

Glycoside phosphorylases (GPs) catalyze the phosphorolysis of glycans into the corresponding sugar 1-phosphates and shortened glycan chains. Given the diversity of natural β-(1→3)-glucans and their wide range of biotechnological applications, the identification of enzymatic tools that can act on β-(1→3)-glucooligosaccharides is an attractive area of research. GP activities acting on β-(1→3)-glucooligosaccharides have been described in bacteria, the photosynthetic excavate Euglena gracilis, and the heterokont Ochromonas spp. Previously, we characterized β-(1→3)-glucan GPs from bacteria and E. gracilis, leading to their classification in glycoside hydrolase family GH149. Here, we characterized GPs from Gram-positive bacteria and heterokont algae acting on β-(1→3)-glucooligosaccharides. We identified a phosphorylase sequence from Ochromonas spp. (OcP1) together with its orthologs from other species, leading us to propose the establishment of a new GH family, designated GH161. To establish the activity of GH161 members, we recombinantly expressed a bacterial GH161 gene sequence (PapP) from the Gram-positive bacterium Paenibacillus polymyxa ATCC 842 in Escherichia coli We found that PapP acts on β-(1→3)-glucooligosaccharide acceptor...Continue Reading

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Citations

Mar 23, 2021·Frontiers in Plant Science·Malika ChabiUgo Cenci
May 11, 2021·Applied Microbiology and Biotechnology·Zorica UbiparipTom Desmet
Aug 16, 2021·Carbohydrate Research·Gregory S BulmerJolanda M van Munster

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Datasets Mentioned

BETA
BAU78234.1
ACJ76363.1
CP001185.1

Methods Mentioned

BETA
gel filtration
PCR

Software Mentioned

BLAST
PhyML
BLASTP
trimAl
GraphPad Prism
tBLASTn
PSI
Jalview
Chromeleon®
PSORTb

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