Glycosynthase activity of hybrid aspen xyloglucan endo-transglycosylase PttXET16-34 nucleophile mutants

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Title Glycosynthase activity of hybrid aspen xyloglucan endo-transglycosylase PttXET16-34 nucleophile mutants
Author Piens, Kathleen; Henriksson, Anna-Maria; Gullfot, Fredrika; Lopez, Marie; Fauré, Régis; Ibatullin, Farid M.; Teeri, Tuula T.; Driguez, Hugues; Brumer, Harry
Journal Name Organic and Biomolecular Chemistry
Editor Dr. Vikki Allen
Year Published 2007
Place of publication United Kingdom
Publisher Royal Society of Chemistry
Abstract Glycosynthases are active-site mutants of glycoside hydrolases that catalyse glycosyl transfer using suitable activated donor substrates without competing product hydrolysis (S. M. Hancock, M. D. Vaughan and S. G. Withers, Curr. Opin. Chem. Biol., 2006, 10, 509–519). Site-directed mutagenesis of the catalytic nucleophile, Glu-85, of a Populus tremula x tremuloides xyloglucan endo-transglycosylase (PttXET16-34, EC 2.4.1.207) into alanine, glycine, and serine yielded enzymes with glycosynthase activity. Product analysis indicated that PttXET16-34 E85A in particular was able to catalyse regio- and stereospecific homo- and hetero-condensations of -xylogluco-oligosaccharyl fluoride donors XXXGF and XLLGF to produce xyloglucans with regular sidechain substitution patterns. This substrate promiscuity contrasts that of the Humicola insolens Cel7B E197A glycosynthase, which was not able to polymerise the di-galactosylated substrate XLLGF. The production of the PttXET16-34 E85A xyloglucosynthase thus expands the repertoire of glycosynthases to include those capable of synthesising structurally homogenenous xyloglucans for applications.
Peer Reviewed Yes
Published Yes
Alternative URI http://dx.doi.org/10.1039/b714570e
Volume 5
Page from 3971
Page to 3978
ISSN 1477-0520
Date Accessioned 2009-08-19
Date Available 2009-12-05T05:16:25Z
Language en_AU
Faculty Faculty of Science, Environment, Engineering and Technology
Subject Organic Chemical Synthesis
URI http://hdl.handle.net/10072/27096
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1x

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