Information on EC - dolichyl-phosphooligosaccharide-protein glycotransferase

for references in articles please use BRENDA:EC2.4.99.21
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IUBMB Comments
The enzyme, characterized from the archaea Methanococcus voltae and Haloferax volcanii, transfers a glycan component from dolichyl phosphooligosaccharide to external proteins. It is different from EC, dolichyl-diphosphooligosaccharide-protein glycotransferase, which uses dolichyl diphosphate as carrier compound in bacteria and eukaryotes. The enzyme participates in the N-glycosylation of proteins in some archaea. It requires Mn2+. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60), it is alpha,omega-saturated and it may have additional unsaturated positions in the chain.
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The enzyme appears in viruses and cellular organisms
AF_0380, AglB, AglB protein, AglB-L, aglB1, AlgB, archaeal oligosaccharyl transferase, dolichyl-monophosphooligosaccharide-protein glycotransferase, Mv1749, MVO1749, more
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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