1. New insight into the mode of action of a GH74 xyloglucanase on tamarind seed xyloglucan: Action pattern and cleavage site.
- Author
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Chen, Mingrui, Ropartz, David, Mac-Béar, Jessica, Bonnin, Estelle, and Lahaye, Marc
- Subjects
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PLANT cell walls , *HYDROLASES , *XYLOGLUCANS - Abstract
Structural elucidation of plant cell wall xyloglucan through the analysis of enzymatically produced fragments requires detailed knowledge of enzymes hydrolytic mechanism. In this note, the mode of action and cleavage site of commercial recombinant xyloglucanases (GH74, Paenibacillus sp.) was studied on native and fluorescent-tagged tamarind xyloglucan. In complement to information provided by the manufacturer, GH74 hydrolysis was shown dual endo/exo- and exo-processive with low affinity towards labelled reducing-ends. GH74 accommodated X/G in its subsite −1 and X/L in its subsite +1. Moreover, hydrolysis kinetic indicated a GH74 activity inhibition by excess products. These results will help for application of this enzyme in xyloglucans structural analysis or for processing cell walls. [Display omitted] • GH74-xyloglucanase (Paenibacillus sp) showed endo-/exo-processive hydrolysis pattern. • GH74 activity was inhibited by excess hydrolysis products. • GH74 accommodated X/G unit in subsite −1 and X/L unit in subsite +1 for its cleavage. [ABSTRACT FROM AUTHOR]
- Published
- 2022
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