Growth of Chitinophaga pinensis on Plant Cell Wall Glycans and Characterisation of a Glycoside Hydrolase Family 27 beta-L-Arabinopyranosidase Implicated in Arabinogalactan Utilisation
2015 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 10, no 10, e0139932Article in journal (Refereed) Published
The genome of the soil bacterium Chitinophaga pinensis encodes a diverse array of carbohydrate active enzymes, including nearly 200 representatives from over 50 glycoside hydrolase (GH) families, the enzymology of which is essentially unexplored. In light of this genetic potential, we reveal that C. pinensis has a broader saprophytic capacity to thrive on plant cell wall polysaccharides than previously reported, and specifically that secretion of beta-L-arabinopyranosidase activity is induced during growth on arabinogalactan. We subsequently correlated this activity with the product of the Cpin_5740 gene, which encodes the sole member of glycoside hydrolase family 27 (GH27) in C. pinensis, CpArap27. Historically, GH27 is most commonly associated with alpha-D-galactopyranosidase and alpha-D-N-acetylgalactosaminidase activity. A new phylogenetic analysis of GH27 highlighted the likely importance of several conserved secondary structural features in determining substrate specificity and provides a predictive framework for identifying enzymes with the less common beta-L-arabinopyranosidase activity.
Place, publisher, year, edition, pages
[McKee, Lauren S.; Brumer, Harry] Royal Inst Technol KTH, AlbaNova Univ Ctr, Div Glycosci, Sch Biotechnol, S-10691 Stockholm, Sweden. [McKee, Lauren S.; Brumer, Harry] Wallenberg Wood Sci Ctr, S-10044 Stockholm, Sweden. [Brumer, Harry] Univ British Columbia, Michael Smith Labs, Vancouver, BC V6T 1Z4, Canada. [Brumer, Harry] Univ British Columbia, Dept Chem, Vancouver, BC V6T 1Z4, Canada., 2015. Vol. 10, no 10, e0139932
Medical Biotechnology Medical Biotechnology
IdentifiersURN: urn:nbn:se:kth:diva-176339DOI: 10.1371/journal.pone.0139932ISI: 000362511000066PubMedID: 26448175ScopusID: 2-s2.0-84948698182OAI: oai:DiVA.org:kth-176339DiVA: diva2:868029
QC 201511092015-11-092015-11-032015-11-09Bibliographically approved