Reaction: UDP-α-D-glucuronate + an archaeal dolichyl α-D-glucosyl phosphate = UDP + an archaeal dolichyl β-D-glucuronosyl-(1→4)-α-D-glucosyl phosphate
Other name(s): aglG (gene name)
Systematic name: UDP-α-D-glucuronate:dolichyl phosphate glucuronosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from the halophilic archaeon Haloferax volcanii, participates in the protein N-glycosylation pathway. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60) and is α,ω-saturated. However, in vitro the enzyme was also able to act on a substrate with an unsaturated end.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Yurist-Doutsch, S., Abu-Qarn, M., Battaglia, F., Morris, H.R., Hitchen, P.G., Dell, A. and Eichler, J. aglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein. Mol. Microbiol. 69 (2008) 1234-1245. [PMID: 18631242]
2. Elharar, Y., Podilapu, A.R., Guan, Z., Kulkarni, S.S. and Eichler, J. Assembling glycan-charged dolichol phosphates: chemoenzymatic synthesis of a Haloferax volcanii N-glycosylation pathway intermediate. Bioconjug Chem 28 (2017) 2461-2470. [PMID: 28809486]