EC 3 - Hydrolases
EC 3.2 - Glycosylases
EC 3.2.1 - Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds
EC 3.2.1.177 - α-D-xyloside xylohydrolase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 3.2.1.177
Names
Accepted name:
α-D-xyloside xylohydrolase
Other
name:
α-xylosidase
Systematic name:
α-D-xyloside xylohydrolase
Reaction
- Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.
Comments:
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
Gene Ontology:
GO:0061634
UniProtKB/Swiss-Prot:
AGDD_EMENI
GH31A_BACO1
XYL1_ARATH
XYL2_ARATH
XYLA_ASPNC
XYLQ_LACPE
XYLS_ECOLI
XYLS_SACS2
References
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Identification and molecular characterization of the first α-xylosidase from an archaeon.J. Biol. Chem. 275 : 22082-22089 (2000). [PMID: 10801892]
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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]
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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]
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Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate.J. Biol. Chem. 280 : 2105-2115 (2005). [PMID: 15501829]
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Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana.Plant Cell Physiol. 47 : 55-63 (2006). [PMID: 16267099]
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Structural elements to convert Escherichia coli α-xylosidase (YicI) into α-glucosidase.FEBS Lett. 580 : 2707-2711 (2006). [PMID: 16631751]
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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 3.2.1.177 created 2011]