EC 18.104.22.168 - α-D-xyloside xylohydrolase
IntEnz Enzyme Nomenclature
- Hydrolysis of terminal, non-reducing α-D-xylose residues with release of α-D-xylose.
The enzyme catalyses hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide. Representative α-xylosidases from glycoside hydrolase family 31 utilize a two-step (double-displacement) mechanism involving a covalent glycosyl-enzyme intermediate, and retain the anomeric configuration of the product.
Links to other databases
Identification and molecular characterization of the first α-xylosidase from an archaeon.J. Biol. Chem. 275: 22082-22089 (2000). [PMID: 10801892]
Cloning and expression pattern of a gene encoding an α-xylosidase active against xyloglucan oligosaccharides from Arabidopsis.Plant Physiol. 126: 910-920 (2001). [PMID: 11402218]
Molecular characterisation of a xyloglucan oligosaccharide-acting α-D-xylosidase from nasturtium (Tropaeolum majus L.) cotyledons that resembles plant 'apoplastic' α-D-glucosidases.Planta 214: 406-413 (2002). [PMID: 11859845]
Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate.J. Biol. Chem. 280: 2105-2115 (2005). [PMID: 15501829]
Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana.Plant Cell Physiol. 47: 55-63 (2006). [PMID: 16267099]
Structural elements to convert Escherichia coli α-xylosidase (YicI) into α-glucosidase.FEBS Lett. 580: 2707-2711 (2006). [PMID: 16631751]
Structural and enzymatic characterization of a glycoside hydrolase family 31 α-xylosidase from Cellvibrio japonicus involved in xyloglucan saccharification.Biochem. J. 436: 567-580 (2011). [PMID: 21426303]
[EC 22.214.171.124 created 2011]