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Literature summary for 2.4.99.18 extracted from

  • Faridmoayer, A.; Fentabil, M.A.; Mills, D.C.; Klassen, J.S.; Feldman, M.F.
    Functional characterization of bacterial oligosaccharyltransferases involved in O-linked protein glycosylation (2007), J. Bacteriol., 189, 8088-8098.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas aeruginosa
expression in Escherichia coli Neisseria meningitidis

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis
-
-
-
Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas aeruginosa
-
Neisseria meningitidis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dolichyl diphosphooligosaccharide + protein L-asparagine PglL is able to transfer diverse oligo- and polysaccharides Neisseria meningitidis dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine
-
?
dolichyl diphosphooligosaccharide + protein L-asparagine PilO activity is restricted to short oligosaccharides Pseudomonas aeruginosa dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine
-
?

Synonyms

Synonyms Comment Organism
oligosaccharyltransferase
-
Pseudomonas aeruginosa
oligosaccharyltransferase
-
Neisseria meningitidis
OTase
-
Pseudomonas aeruginosa
OTase
-
Neisseria meningitidis
PglL
-
Neisseria meningitidis
PilO
-
Pseudomonas aeruginosa