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2.4.99.19: undecaprenyl-diphosphooligosaccharide-protein glycotransferase

This is an abbreviated version!
For detailed information about undecaprenyl-diphosphooligosaccharide-protein glycotransferase, go to the full flat file.

Word Map on EC 2.4.99.19

Reaction

tritrans,heptacis-undecaprenyl diphosphooligosaccharide
+
[protein]-L-asparagine
=
tritrans,heptacis-undecaprenyl diphosphate
 +
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine

Synonyms

bacterial oligosaccharyltransferase, bacterial OST, N-oligosaccharyltransferase, N-OTase, oligosaccharyl transferase, oligosaccharyltransferase, oligosacharyltransferase, OST, OT, OTase, PglB, PglB oligosaccharyltransferase, PglB protein, PglB1, PglB2

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.99 Transferring other glycosyl groups
                2.4.99.19 undecaprenyl-diphosphooligosaccharide-protein glycotransferase

Engineering

Engineering on EC 2.4.99.19 - undecaprenyl-diphosphooligosaccharide-protein glycotransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D152E
-
site-directed mutagenesis, D152 and E316 can both be mutated to their acidic counterparts (D152E and E316D) and still retain activity, albeit at a notably decreased level
D475A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
D475E
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
D54A
-
site-directed mutagenesis, the increased Und-PP-Bac-GalNAc substrate concentration has little effect on the mutant activity
E316D
-
site-directed mutagenesis, D152 and E316 can both be mutated to their acidic counterparts (D152E and E316D) and still retain activity, albeit at a notably decreased level
E316Q
-
site-directed mutagenesis, inactive mutant
K478A
D154A
the mutation reduces the observed glycosylation yield by over 50% compared to the wild-type enzyme
D56A
the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme
D56A/E319A
the double mutant is inactive
E319A
the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme
additional information