Jump to content

Xyloglucan:xyloglucosyl transferase

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by BrownHairedGirl (talk | contribs) at 15:51, 29 September 2019 (replace links to deleted portals: Portal:Molecular and Cellular BiologyPortal:Biology). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

xyloglucan:xyloglucosyl transferase
Identifiers
EC no.2.4.1.207
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a xyloglucan:xyloglucosyl transferase (EC 2.4.1.207) is an enzyme that catalyzes the chemical reaction in which a beta-(1,4) bond in the backbone of a xyloglucan in broken; the xyloglucanyl segment is then transferred to the O4 of the non-reducing terminal glucose residue of either xyloglucan or an oligosaccharide thereof.[1]

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is xyloglucan:xyloglucan xyloglucanotransferase. Other names in common use include endo-xyloglucan transferase, and xyloglucan endotransglycosylase.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1UMZ and 1UN1.

References

  1. ^ Thompson, James E.; Fry, Stephen C. (2001). "Restructuring of wall-bound xyloglucan by transglycosylation in living plant cells" (PDF). The Plant Journal. 26 (1): 23–34. doi:10.1046/j.1365-313x.2001.01005.x. PMID 11359607.
  • Fry SC, Smith RC, Renwick KF, Martin DJ, Hodge SK, Matthews KJ. "Xyloglucan endotransglycosylase, a new wall-loosening enzyme activity from plants". Biochem. J. 282 (Pt 3): 821–8. PMC 1130861. PMID 1554366.
  • Nishitani K, Tominaga R (1992). "Endo-xyloglucan transferase, a novel class of glycosyltransferase that catalyzes transfer of a segment of xyloglucan molecule to another xyloglucan molecule". J. Biol. Chem. 267 (29): 21058–64. PMID 1400418.
  • Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM (2006). "A proteomic analysis of arsenical drug resistance in Trypanosoma brucei". Proteomics. 6 (9): 2726–32. doi:10.1002/pmic.200500419. PMID 16526094.
  • Lorences EP, Fry, SC (1993). "Xyloglucan oligosaccharides with at least two alpha-D-xylose residues act as acceptor substrates for xyloglucan endotransglycosylase and promote the depolymerisation of xyloglucan". Plant Physiol. 88: 105–112. doi:10.1111/j.1399-3054.1993.tb01767.x.