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UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase
Identifiers
EC no.	2.6.1.91
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
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PMC	articles
PubMed	articles
NCBI	proteins

UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase (EC 2.6.1.91, pglE (gene)) is an enzyme with systematic name UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine:2-oxoglutarate aminotransferase.^[1]^[2]^[3]^[4] This enzyme catalyses the following chemical reaction

UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine + 2-oxoglutarate

\rightleftharpoons

UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + L-glutamate

This enzyme is a pyridoxal-phosphate protein.

References

^ 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.
^ Schoenhofen IC, McNally DJ, Vinogradov E, Whitfield D, Young NM, Dick S, Wakarchuk WW, Brisson JR, Logan SM (January 2006). "Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways" (PDF). The Journal of Biological Chemistry. 281 (2): 723–32. doi:10.1074/jbc.m511021200. PMID 16286454.
^ 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

UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine+transaminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] 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.

[2] Schoenhofen IC, McNally DJ, Vinogradov E, Whitfield D, Young NM, Dick S, Wakarchuk WW, Brisson JR, Logan SM (January 2006). "Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways" (PDF). The Journal of Biological Chemistry. 281 (2): 723–32. doi:10.1074/jbc.m511021200. PMID 16286454.

[3] 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.

[4] 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.

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