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Literature summary for 2.4.99.18 extracted from
- Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans (2014), Appl. Environ. Microbiol., 80, 486-496.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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 |
| 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 |
| 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)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? |  |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haloarcula marismortui | - |
- |
- |
| Halobacterium salinarum | - |
- |
- |
| Haloferax mediterranei | - |
- |
- |
| Haloferax volcanii | - |
- |
- |
| Haloferax volcanii DSM 3757 | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| AglB | - |
Haloarcula marismortui |
| AglB | - |
Halobacterium salinarum |
| AglB | - |
Haloferax volcanii |
| AglB | - |
Haloferax mediterranei |
| AlgB | - |
Haloarcula marismortui |
| AlgB | - |
Halobacterium salinarum |
| AlgB | - |
Haloferax volcanii |
| AlgB | - |
Haloferax mediterranei |
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