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2.6.1.34 |
| Description |
UDP-N-acetylbacillosamine transaminase |
| Alternative names |
UDP-4-amino-2-acetamido-2,4,6-trideoxyglucose aminotransferase.
UDP-4-amino-2-acetamido-2,4,6-trideoxyglucose transaminase.
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase.
PglE (gene name)
EpsN (gene name)
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| Catalyzed reaction |
UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + L-glutamate |
| Cofactor |
Pyridoxal-phosphate. |
| Comments |
The enzyme is involved in biosynthesis of UDP- N,N'-diacetylbacillosamine, an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species and O-linked glycosylation of certain L-serine residues in Neisseria species.
Formerly EC 2.6.1.91. |
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In C. jejuni PglE is involved in the general glycosylation pathway (Pgl) responsible for the N-linked modification of proteins with a heptasaccharide containing 2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose, a derivative of bacillosamine.
Specifically, the product of the PglE aminotransferase is UDP-4-amino-4,6-dideoxy-alpha-D-GlcNAc (UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose) - a precursor used in the production of the Pgl glycan component |
| PDB |
1O61; 4ZTC; |
| Organisms |
-Eubacteria |
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Family |
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| Links |
Enzyme (activities) 2.6.1.34
BRENDA (activities) 2.6.1.34
KEGG (pathways) 2.6.1.34
PLPMDB (PLP mutants) 2.6.1.34
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| References |
Kaundinya CR, Savithri HS, Rao KK, Balaji PV (2018) EpsN from Bacillus subtilis 168 has UDP 2,6-dideoxy 2-acetamido 4-keto glucose aminotransferase activity in vitro Glycobiology 28 802-812. Riegert AS, Young NM, Watson DC, Thoden JB, Holden HM (2015) Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis Protein Sci 24 1609-16. Morrison, M.J.; Imperiali, B. (2013) Biosynthesis of UDP-N,N'-diacetylbacillosamine in Acinetobacter baumannii: Biochemical characterization and correlation to existing pathways Arch Biochem Biophys 536 72-80. Hartley MD, Morrison MJ, Aas FE, Børud B, Koomey M, Imperiali B (2011) Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N'-diacetylbacillosamine Biochemistry 50 4936-48. Olivier NB, Chen MM, Behr JR, Imperiali B.
(2006) In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system Biochemistry 45 13659-69. Schoenhofen IC, McNally DJ, Vinogradov E, Whitfield D, Young NM, Dick S, Wakarchuk WW, Brisson JR, Logan SM. (2006) Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways J Biol Chem. 281 723-32. |
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| last changed |
2018/12/21 13:21 |
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