Biology:Alpha-D-xyloside xylohydrolase

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Alpha-D-xyloside xylohydrolase
Identifiers
EC number3.2.1.177
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Alpha-D-xyloside xylohydrolase (EC 3.2.1.177, alpha-xylosidase) is an enzyme.[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction

Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.

The enzyme catalyses hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide.

References

  1. "Identification and molecular characterization of the first alpha -xylosidase from an archaeon". The Journal of Biological Chemistry 275 (29): 22082–9. July 2000. doi:10.1074/jbc.M910392199. PMID 10801892. 
  2. "Cloning and expression pattern of a gene encoding an alpha-xylosidase active against xyloglucan oligosaccharides from Arabidopsis". Plant Physiology 126 (2): 910–20. June 2001. doi:10.1104/pp.126.2.910. PMID 11402218. 
  3. "Molecular characterisation of a xyloglucan oligosaccharide-acting alpha-D-xylosidase from nasturtium (Tropaeolum majus L.) cotyledons that resembles plant 'apoplastic' alpha-D-glucosidases". Planta 214 (3): 406–13. January 2002. doi:10.1007/s004250100631. PMID 11859845. 
  4. "Mechanistic and structural analysis of a family 31 alpha-glycosidase and its glycosyl-enzyme intermediate". The Journal of Biological Chemistry 280 (3): 2105–15. January 2005. doi:10.1074/jbc.m410468200. PMID 15501829. 
  5. "Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana". Plant & Cell Physiology 47 (1): 55–63. January 2006. doi:10.1093/pcp/pci223. PMID 16267099. 
  6. "Structural elements to convert Escherichia coli alpha-xylosidase (YicI) into alpha-glucosidase". FEBS Letters 580 (11): 2707–11. May 2006. doi:10.1016/j.febslet.2006.04.025. PMID 16631751. 
  7. "Structural and enzymatic characterization of a glycoside hydrolase family 31 α-xylosidase from Cellvibrio japonicus involved in xyloglucan saccharification". The Biochemical Journal 436 (3): 567–80. June 2011. doi:10.1042/bj20110299. PMID 21426303. https://hal.archives-ouvertes.fr/hal-00596265/file/PEER_stage2_10.1042%252FBJ20110299.pdf. 

External links