N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase: Difference between revisions
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: UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol <math>\rightleftharpoons</math> UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol |
: UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol <math>\rightleftharpoons</math> UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol |
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This enzyme is isolated from ''[[Campylobacter jejuni]]''. It is important for [[N-linked glycosylation|''N''-linked glycosylation]] in this species.<ref>{{cite journal|vauthors=Karlyshev AV, Ketley JM, Wren BW|title=The ''Campylobacter jejuni'' Glycome|journal=FEMS Microbiology Reviews|volume=29|issue=2|pages=377-390|doi=10.1016/j.fmrre.2005.01.003|doi-access=free|pmid=15808749|year=2005}}</ref> The glycosyl motif that the enzymes encoded by the [[Pgl|''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.<ref>{{cite journal|vauthors=Young NM, Brisson JR, Kelly J, Watson DC, Tessier L, Lanthier PH, Jarrell HC, Cadotte N, St Michael F, Aberg E, Szymanski CM|title=Structure of the ''N''-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, ''Campylobacter jejuni''|journal=Journal of Biological Chemistry|volume=277|issue=45|pages=42530-42539|year=2002|doi=10.1074/jbc.M206114200|doi-access=free|pmid=12186869}}</ref> Glycosylation takes place on an [[undecaprenyl pyrophosphate]] on the cytosolic face of the plasma membrane, followed by [[ABC transporter]]–mediated transfer to the periplasmic space (a "flop") and en bloc transfer to an [[asparagine]] residue.<ref>{{cite journal|vauthors=Alaimo C, Catrein I, Morf L, Marolda CL, Callewaert N, Valvano MA, Feldman MF, Aebi M|title=Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides|journal=The EMBO Journal|volume=25|issue=5|pages=967-976|year=2006|doi=10.1038/sj.emboj.7601024|doi-access=free|pmid=16498400|pmc=1409731}}</ref> |
This enzyme is isolated from ''[[Campylobacter jejuni]]''. It is important for [[N-linked glycosylation|''N''-linked glycosylation]] in this species.<ref>{{cite journal|vauthors=Karlyshev AV, Ketley JM, Wren BW|title=The ''Campylobacter jejuni'' Glycome|journal=FEMS Microbiology Reviews|volume=29|issue=2|pages=377-390|doi=10.1016/j.fmrre.2005.01.003|doi-access=free|pmid=15808749|year=2005}}</ref> The glycosyl motif that the enzymes encoded by the [[Pgl|''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.<ref>{{cite journal|vauthors=Young NM, Brisson JR, Kelly J, Watson DC, Tessier L, Lanthier PH, Jarrell HC, Cadotte N, St Michael F, Aberg E, Szymanski CM|title=Structure of the ''N''-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, ''Campylobacter jejuni''|journal=Journal of Biological Chemistry|volume=277|issue=45|pages=42530-42539|year=2002|doi=10.1074/jbc.M206114200|doi-access=free|pmid=12186869}}</ref> Glycosylation takes place on an [[undecaprenyl pyrophosphate]] on the cytosolic face of the plasma membrane, followed by [[ABC transporter]]–mediated transfer to the periplasmic space (a "[[flippase|flop]]") and en bloc transfer to an [[asparagine]] residue.<ref>{{cite journal|vauthors=Alaimo C, Catrein I, Morf L, Marolda CL, Callewaert N, Valvano MA, Feldman MF, Aebi M|title=Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides|journal=The EMBO Journal|volume=25|issue=5|pages=967-976|year=2006|doi=10.1038/sj.emboj.7601024|doi-access=free|pmid=16498400|pmc=1409731}}</ref> |
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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.<ref name=glover2005/> |
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.<ref name=glover2005/> |
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Revision as of 21:48, 16 May 2024
| 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 | ||||||||
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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 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 ABC transporter–mediated transfer to the periplasmic space (a "flop") 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
- ^ a b 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.
- ^ 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.
- ^ 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.
- ^ 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)
