UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase (EC 2.3.1.203, PGLD) is an enzyme with systematic name acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase.[1][2][3] This enzyme catalyses the following chemical reaction
| UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.203 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine CoA + UDP-N,N'-diacetylbacillosamine
UDP-N,N'-diacetylbacillosamine is an intermediate in protein glycosylation pathways in several bacterial species.
References
edit- ^ Olivier NB, Chen MM, Behr JR, Imperiali B (November 2006). "In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system". Biochemistry. 45 (45): 13659–69. doi:10.1021/bi061456h. PMC 2542654. PMID 17087520.
- ^ Rangarajan ES, Ruane KM, Sulea T, Watson DC, Proteau A, Leclerc S, Cygler M, Matte A, Young NM (February 2008). "Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni". Biochemistry. 47 (7): 1827–36. doi:10.1021/bi702032r. PMID 18198901.
- ^ Hartley MD, Morrison MJ, Aas FE, Børud B, Koomey M, Imperiali B (June 2011). "Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N'-diacetylbacillosamine". Biochemistry. 50 (22): 4936–48. doi:10.1021/bi2003372. PMC 3108506. PMID 21542610.
External links
edit- UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine+N-acetyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
