EC Number |
General Information |
Reference |
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2.4.1.292 | evolution |
genotyping, overview. The variable presence of two open reading frames (ORFs) in the pgl locus includes a putative glycosyltransferase gene, pglG, in addition to a glucosyltransferase-expressing gene, pglH. Polymorphisms exist at the gene level described for pglH and pglH2, where only one nonsynonymous mutation is accountable for the glycoform switch from Glc to GlcNAc. lacking these two ORFs retain the first 40 bp of pglG and the last 100 bp of pglH. Homologous recombination within the pgl loci, through genomic analysis of 100 African serogroup A isolates in Ethiopia in 2014, is detected representing the clonal replacement of hypervirulent meningococcal clone sequence type 7 (ST-7) by the ST-2859 descendant clone. Major polymorphism in pgl gene content within a small geographic area. This recombination event seems to emphasizes the role of protein glycosylation diversity in immune evasion. Polymorphisms exist at the gene level described for pglH and pglH2, where only one nonsynonymous mutation is accountable for the glycoform switch from Glc to GlcNAc. One subcluster has pglH while the other has the pglH2 variant allele |
759430 |
2.4.1.292 | evolution |
PglH is a glycosyltransferase protein containing the conserved EX7E sequence motif |
718851 |
2.4.1.292 | evolution |
PglH is a GT-B family member |
759837 |
2.4.1.292 | malfunction |
pgl genotypes and glycosylation phenotypes in meningococcal isolates and the changes occurring during short-term asymptomatic carriage, overview. Polymorphisms exist at the gene level described for pglH and pglH2, where only one nonsynonymous mutation is accountable for the glycoform switch from Glc to GlcNAc |
759430 |
2.4.1.292 | malfunction |
pglH mutants have significantly reduced ability to adhere to and invade human epithelial Caco-2 cells, the 81116 pglH mutant is also severely affected in its ability to colonize chicks |
-, 720384 |
2.4.1.292 | malfunction |
polymorphisms in PglH are associated with diminished glycosyltransferase activity |
720929 |
2.4.1.292 | metabolism |
PglH is involved in the N-linked glycan structure formation, which is realized through a series of sequential glycosyl transfer reactions from uridine diphosphate-activated sugars to an undecaprenyl diphosphate carrier. Once undecaprenyl-diphospho-Bac2,4diNAc is formed by PglC, PglF, PglE, and PglD, sequential N-acetyl-galactosamine transfer reactions are catalyzed by PglA, PglJ and PglH to provide undecaprenyldiphospho-Bac2,4diNAc-GalNAc, undecaprenyldiphospho-Bac2,4diNAc-(GalNAc)2 and undecaprenyldiphospho-Bac2,4diNAc-(GalNAc)5, respectively |
718851 |
2.4.1.292 | metabolism |
PglH is part of a general N-linked glycosylation pathway, encoded by the pgl gene cluster, which culminates in the transfer of a heptasaccharide: GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-Bac, where Bac is bacillosamine (2,4-diacetamido-2,4,6-trideoxyglucose), from a membrane-anchored undecaprenylpyrophosphate-linked donor to the asparagine side chain of proteins at the Asn-X-Ser/Thr motif. The glycosyltransferases, PglA, PglH, PglI, and PglJ, responsible for the biosynthesis of the Und-PP-linked heptasaccharide. Elongation of the trisaccharide with PglH results in a hexasaccharide revealing the polymerase activity of PglH |
-, 720888 |
2.4.1.292 | metabolism |
the membrane-associated, processive and retaining glycosyltransferase PglH from Campylobacter jejuni is part of the biosynthetic pathway of the lipid-linked oligosaccharide (LLO) that serves as the glycan donor in bacterial protein N-glycosylation |
759837 |
2.4.1.292 | metabolism |
the Pgl pathway produces the N-linked glycan heptasaccharide GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-Bac2,4diNAc-1-Asn. The pathway begins with pyrophosphate bond formation between the Bac2,4diNAc phosphate and undecaprenylphosphate by Cj1124c (PglC) to form Bac2,4diNAc-alpha1-PP-Und. One N-acetylgalactosamine is linked to the polyisoprenediphosphate-bound N,N'-diacetylbacillosamine by Cj1125c (PglA) to form GalNAc-alpha1,3-Bac2,4diNAc-alpha1-PP-Und. Next, four additional GalNAc and one branching glucose are added sequentially to the isoprene-linked disaccharide by PglJ, PglH, and PglI, to form the heptasaccharide, overview |
-, 714160 |