N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase

N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase
Identifiers
EC no.	2.4.1.290
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase (EC 2.4.1.290, PglA) is an enzyme with systematic name UDP-N-acetyl-alpha-D-galactosamine:N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-alpha-N-acetyl-D-galactosaminyltransferase. ^[1] This enzyme catalyses the following chemical reaction

UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol ${\displaystyle \rightleftharpoons }$ UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol

This enzyme is isolated from Campylobacter jejuni . It is important for N-linked glycosylation in this species. ^[2] The glycosyl motif that the enzymes encoded by the Pgl locus create consists of a bacillosamine joined to a GalNAc residue by an alpha 1–3 glycosidic bond, followed by four additional GalNAc residues linked by alpha 1–4 bonds. A branching glucose residue completes the heptasaccharide, joined by a beta 1–3 linkage to the third GalNAc residue from the amino acid linkage point. ^[3] Glycosylation takes place on an undecaprenyl pyrophosphate on the cytosolic face of the plasma membrane, followed by flippase transfer to the periplasmic space and en bloc transfer to an asparagine residue. ^[4]

This enzyme catalyzes the addition of GalNAc, covalently bonded to carrier uridine diphosphate (UDP), to isoprenoid lipid–linked bacillosamine, resulting in production of UDP and the glycosylated lipid. ^[1]

References

1. Glover KJ, Weerapana E, Imperiali B (October 2005). "In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation". Proceedings of the National Academy of Sciences of the United States of America. 102 (40): 14255–9. Bibcode:2005PNAS..10214255G. doi: 10.1073/pnas.0507311102 . PMC   1242339 . PMID   16186480.
2. Karlyshev AV, Ketley JM, Wren BW (2005). "The Campylobacter jejuni Glycome". FEMS Microbiology Reviews. 29 (2): 377–390. doi: 10.1016/j.fmrre.2005.01.003 . PMID   15808749.
3. Young NM, Brisson JR, Kelly J, Watson DC, Tessier L, Lanthier PH, Jarrell HC, Cadotte N, St Michael F, Aberg E, Szymanski CM (2002). "Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni". Journal of Biological Chemistry. 277 (45): 42530–42539. doi: 10.1074/jbc.M206114200 . PMID   12186869.
4. Alaimo C, Catrein I, Morf L, Marolda CL, Callewaert N, Valvano MA, Feldman MF, Aebi M (2006). "Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides". The EMBO Journal. 25 (5): 967–976. doi: 10.1038/sj.emboj.7601024 . PMC   1409731 . PMID   16498400.

External links

• N,N'-diacetylbacillosaminyl-diphospho-undecaprenol+alpha-1,3-N-acetylgalactosaminyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)