| EC |
2.4.1.356 |
| Accepted name: |
glucosyl-dolichyl phosphate glucuronosyltransferase |
| 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 |
| 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. [DOI] [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. Bioconjugate Chem. 28 (2017) 2461–2470. [DOI] [PMID: 28809486] |
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| [EC 2.4.1.356 created 2018] |
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