Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.B58 extracted from

  • Cohen-Rosenzweig, C.; Yurist-Doutsch, S.; Eichler, J.
    AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase (2012), J. Bacteriol., 194, 6909-6916.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.B58

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane multispanning membrane protein Haloferax volcanii 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein Haloferax volcanii the enzyme is involved in the assembly a pentasaccharide to selected Asn residues of the S-layer glycoprotein in the archaeal N-glycosylation pathway dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein
-
 ?
dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein Haloferax volcanii DSM 3757 the enzyme is involved in the assembly a pentasaccharide to selected Asn residues of the S-layer glycoprotein in the archaeal N-glycosylation pathway dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein
-
 ?

Organism

Organism UniProt Comment Textmining
Haloferax volcanii D4GYH0
-
-
Haloferax volcanii DSM 3757 D4GYH0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein the enzyme is involved in the assembly a pentasaccharide to selected Asn residues of the S-layer glycoprotein in the archaeal N-glycosylation pathway Haloferax volcanii dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein
-
 ?
dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein cells lacking HVO_1526 do not present peaks corresponding to the pentasaccharide-modified Asn-13-containing peptide. When cells of the deletion strain are transformed to express a polyhistidine-tagged version of HVO_1526, it is observed that the Asn-13-containing S-layer glycoprotein-derived peptide is once again modified by the complete pentasaccharide Haloferax volcanii dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein
-
 ?
dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein the enzyme is involved in the assembly a pentasaccharide to selected Asn residues of the S-layer glycoprotein in the archaeal N-glycosylation pathway Haloferax volcanii DSM 3757 dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein
-
 ?
dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein cells lacking HVO_1526 do not present peaks corresponding to the pentasaccharide-modified Asn-13-containing peptide. When cells of the deletion strain are transformed to express a polyhistidine-tagged version of HVO_1526, it is observed that the Asn-13-containing S-layer glycoprotein-derived peptide is once again modified by the complete pentasaccharide Haloferax volcanii DSM 3757 dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein
-
 ?

Synonyms

Synonyms Comment Organism
AglS
-
 Haloferax volcanii
HVO_1526 locus name Haloferax volcanii

General Information

General Information Comment Organism
malfunction cells lacking HVO_1526 do not present peaks corresponding to the pentasaccharide-modified Asn-13-containing peptide. When cells of the deletion strain are transformed to express a polyhistidine-tagged version of HVO_1526, it is observed that the Asn-13-containing S-layer glycoprotein-derived peptide is once again modified by the complete pentasaccharide Haloferax volcanii
physiological function the enzyme is involved in the archaeal N-glycosylation pathway Haloferax volcanii