Jump to content

Dolichyl-diphosphooligosaccharide–protein glycotransferase

From Wikipedia, the free encyclopedia
(Redirected from STT3)
dolichyl-diphosphooligosaccharide-protein glycotransferase
Identifiers
EC no.2.4.99.18
CAS no.75302-32-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Oligosaccaryltransferase
Identifiers
Symbol?
InterProIPR018943
OPM superfamily242
OPM protein2lat
Membranome275

In enzymology, a dolichyl-diphosphooligosaccharide–protein glycotransferase (EC 2.4.99.18) is an enzyme that catalyzes the chemical reaction

dolichyl diphosphooligosaccharide + protein L-asparagine dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine

Thus, the two substrates of this enzyme are dolichyl diphosphooligosaccharide and protein L-asparagine, whereas its 3 products are dolichyl diphosphate, glycoprotein with the oligosaccharide chain attached by N-glycosyl, and linkage to protein L-asparagine.

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is dolichyl-diphosphooligosaccharide:protein-L-asparagine oligopolysaccharidotransferase. Other names in common use include dolichyldiphosphooligosaccharide-protein glycosyltransferase, asparagine N-glycosyltransferase, dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase, dolichylpyrophosphodiacetylchitobiose-protein glycosyltransferase, oligomannosyltransferase, oligosaccharide transferase, dolichyldiphosphoryloligosaccharide-protein, and oligosaccharyltransferase. This enzyme participates in n-glycan biosynthesis and glycan structures - biosynthesis 1.

References

[edit]
  • Das RC, Heath EC (1980). "Dolichyldiphosphoryloligosaccharide--protein oligosaccharyltransferase; solubilization, purification, and properties". Proc. Natl. Acad. Sci. U.S.A. 77 (7): 3811–5. Bibcode:1980PNAS...77.3811D. doi:10.1073/pnas.77.7.3811. PMC 349716. PMID 6933437.