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Literature summary extracted from

  • Cohen-Rosenzweig, C.; Guan, Z.; Shaanan, B.; Eichler, J.
    Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans (2014), Appl. Environ. Microbiol., 80, 486-496.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.99.18 despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloarcula marismortui can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB Haloarcula marismortui
2.4.99.18 despite processing distinct lipid-linked glycans in their native hosts, AglB from Halobacterium salinarum can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB Halobacterium salinarum
2.4.99.18 despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloferax mediterranei can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB Haloferax mediterranei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine Haloarcula marismortui
-
 dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine Halobacterium salinarum
-
 dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine Haloferax volcanii
-
 dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine Haloferax mediterranei
-
 dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine Haloferax volcanii DSM 3757
-
 dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.99.18 Haloarcula marismortui
-
-
-
2.4.99.18 Halobacterium salinarum
-
-
-
2.4.99.18 Haloferax mediterranei
-
-
-
2.4.99.18 Haloferax volcanii
-
-
-
2.4.99.18 Haloferax volcanii DSM 3757
-
-
-
2.4.99.21 Haloarcula marismortui
-
-
-
2.4.99.21 Halobacterium salinarum B0R4T2
-
-
2.4.99.21 Halobacterium salinarum DSM 671 B0R4T2
-
-
2.4.99.21 Haloferax mediterranei
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine
-
 Haloarcula marismortui dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine
-
 Halobacterium salinarum dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine
-
 Haloferax volcanii dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine
-
 Haloferax mediterranei dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloarcula marismortui can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB Haloarcula marismortui dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB Haloferax volcanii dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine despite processing distinct lipid-linked glycans in their native hosts, AglB from Halobacterium salinarum can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB Halobacterium salinarum dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloferax mediterranei can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB Haloferax mediterranei dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine haloarchaeal AglB proteins display substrate promiscuity. Haloferax volcanii, Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei AglB each contain distinct glycan-charged lipid carriers. Haloferax volcanii can be functionally replaced by its haloarchaeal homologues Haloarcula marismortui dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine haloarchaeal AglB proteins display substrate promiscuity. Haloferax volcanii, Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei AglB each contain distinct glycan-charged lipid carriers. Haloferax volcanii can be functionally replaced by its haloarchaeal homologues Halobacterium salinarum dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine haloarchaeal AglB proteins display substrate promiscuity. Haloferax volcanii, Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei AglB each contain distinct glycan-charged lipid carriers. Haloferax volcanii can be functionally replaced by its haloarchaeal homologues Haloferax volcanii dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine haloarchaeal AglB proteins display substrate promiscuity. Haloferax volcanii, Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei AglB each contain distinct glycan-charged lipid carriers. Haloferax volcanii can be functionally replaced by its haloarchaeal homologues Haloferax mediterranei dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine
-
 Haloferax volcanii DSM 3757 dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei can readily replace their counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of aglB Haloferax volcanii DSM 3757 dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine haloarchaeal AglB proteins display substrate promiscuity. Haloferax volcanii, Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei AglB each contain distinct glycan-charged lipid carriers. Haloferax volcanii can be functionally replaced by its haloarchaeal homologues Haloferax volcanii DSM 3757 dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.99.18 AglB
-
 Haloarcula marismortui
2.4.99.18 AglB
-
 Halobacterium salinarum
2.4.99.18 AglB
-
 Haloferax volcanii
2.4.99.18 AglB
-
 Haloferax mediterranei
2.4.99.18 AlgB
-
 Haloarcula marismortui
2.4.99.18 AlgB
-
 Halobacterium salinarum
2.4.99.18 AlgB
-
 Haloferax volcanii
2.4.99.18 AlgB
-
 Haloferax mediterranei
2.4.99.21 AglB
-
 Haloarcula marismortui
2.4.99.21 AglB
-
 Haloferax mediterranei
2.4.99.21 AglB
-
 Halobacterium salinarum

General Information

EC Number General Information Comment Organism
2.4.99.21 physiological function enzyme can readily replace its counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of glycotransferase aglB Haloarcula marismortui
2.4.99.21 physiological function enzyme can readily replace its counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of glycotransferase aglB Haloferax mediterranei
2.4.99.21 physiological function enzyme can readily replace its counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of glycotransferase aglB Halobacterium salinarum