Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the newly-formed chain end after endo-initiation on a polymer molecule
Comment
The enzyme removes branched oligosaccharides, containing preferentially four glucoside residues in the main chain, from xyloglucan molecules in a processive manner after the initial endo-type attack on a polysaccharide [1-5]. Hydrolysis occurs at either the unsubstituted D-glucopyranose residue in the main backbone and/or the D-glucopyranose residue bearing a xylosyl group [1-5]. The enzyme does not display activity, or shows very low activity, towards other beta-D-glucans [1,2,4,5].
History
EC 3.2.1.155 created 2005, withdrawn at public-review stage, modified and reinstated 2006, modified 2020
Ichinose H, Araki Y, Michikawa M, Harazono K, Yaoi K, Karita S, Kaneko S
Title
Characterization of an endo-processive-type xyloglucanase having a beta-1,4-glucan-binding module and an endo-type xyloglucanase from Streptomyces avermitilis.
Arnal G, Stogios PJ, Asohan J, Skarina T, Savchenko A, Brumer H
Title
Structural enzymology reveals the molecular basis of substrate regiospecificity and processivity of an exemplar bacterial glycoside hydrolase family 74 endo-xyloglucanase.
Additional sequence and structural characterization of an endo-processive GH74 xyloglucanase from Myceliophthora thermophila and the revision of the EC 3.2.1.155 entry.
