N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase
N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase | |||||||||
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Identifiers | |||||||||
EC number | 2.4.1.291 | ||||||||
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-acetylgalactosamine-N, N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase (EC 2.4.1.291, PglJ) is an enzyme with systematic name UDP-N-acetyl-alpha-D-galactosamine:N-acetylgalactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-alpha-N-acetyl-D-galactosaminyltransferase.[1][2] This enzyme catalyses the following chemical reaction
- UDP-N-acetyl-alpha-D-galactosamine + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol UDP + N-acetyl-D-galactosaminyl-alpha-(1->4)-N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
This enzyme is isolated from Campylobacter jejuni.
References
- ↑ Glover, K.J.; Weerapana, E.; Imperiali, B. (2005). "In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation". Proc. Natl. Acad. Sci. USA. 102 (40): 14255–14259. doi:10.1073/pnas.0507311102. PMC 1242339. PMID 16186480.
- ↑ Chen, M.M.; Weerapana, E.; Ciepichal, E.; Stupak, J.; Reid, C.W.; Swiezewska, E.; Imperiali, B. (2007). "Polyisoprenol specificity in the Campylobacter jejuni N-linked glycosylation pathway". Biochemistry. 46 (50): 14342–14348. doi:10.1021/bi701956x. PMC 2585822. PMID 18034500.
External links
- N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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