Literature summary for 2.4.99.18 extracted from

Jervis, A.J.; Langdon. R.; Hitchen, P.; Lawson, A.J.; Wood, A.; Fothergill, J.L.; Morris, H.R.; Dell, A.; Wren, B.; Linton, D.
Characterization of N-linked protein glycosylation in Helicobacter pullorum (2010), J. Bacteriol., 192, 5228-5236.

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Cloned(Commentary)

Cloned (Comment)	Organism
Helicobacter species contain two unrelated pglB genes (pglB1 and pglB2), neither of which is located within a larger locus involved in protein glycosylation. In complementation experiments, the Helicobacter pullorum PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli	Helicobacter pullorum

Organism

Organism	UniProt	Comment	Textmining
Helicobacter pullorum	E1B265	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Helicobacter pullorum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the PglB1-dependent N-glycosylation with a linear pentasaccharide requires an acidic residue at the -2 position of the N-glycosylation sequon	Helicobacter pullorum	?	-	?

Synonyms

Synonyms	Comment	Organism
PglB1	-	Helicobacter pullorum

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Release 2023.1 (January 2023)