EC |
2.3.1.203 |
Accepted name: |
UDP-N-acetylbacillosamine N-acetyltransferase |
Reaction: |
acetyl-CoA + UDP-N-acetylbacillosamine = CoA + UDP-N,N′-diacetylbacillosamine |
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For diagram of legionaminic acid biosynthesis, click here |
Glossary: |
UDP-N-acetylbacillosamine = UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine
UDP-N,N′-diacetylbacillosamine = UDP-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose |
Other name(s): |
UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase; pglD (gene name) |
Systematic name: |
acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase |
Comments: |
The product, UDP-N,N′-diacetylbacillosamine, is an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species [1,2] and O-linked glycosylation of certain L-serine residues in Neisseria species [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Olivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B. In vitro biosynthesis of UDP-N,N′-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry 45 (2006) 13659–13669. [DOI] [PMID: 17087520] |
2. |
Rangarajan, E.S., Ruane, K.M., Sulea, T., Watson, D.C., Proteau, A., Leclerc, S., Cygler, M., Matte, A. and Young, N.M. 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 (2008) 1827–1836. [DOI] [PMID: 18198901] |
3. |
Hartley, M.D., Morrison, M.J., Aas, F.E., Borud, B., Koomey, M. and Imperiali, B. Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N′-diacetylbacillosamine. Biochemistry 50 (2011) 4936–4948. [DOI] [PMID: 21542610] |
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[EC 2.3.1.203 created 2012, modified 2013] |
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EC |
2.5.1.101 |
Accepted name: |
N,N′-diacetyllegionaminate synthase |
Reaction: |
2,4-diacetamido-2,4,6-trideoxy-α-D-mannopyranose + phosphoenolpyruvate + H2O = N,N′-diacetyllegionaminate + phosphate |
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For diagram of legionaminic acid biosynthesis, click here |
Glossary: |
legionaminate = 5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonate |
Other name(s): |
neuB (gene name); legI (gene name) |
Systematic name: |
phosphoenolpyruvate:2,4-diacetamido-2,4,6-trideoxy-α-D-mannopyranose 1-(2-carboxy-2-oxoethyl)transferase |
Comments: |
Requires a divalent metal such as Mn2+. Isolated from the bacteria Legionella pneumophila and Campylobacter jejuni, where it is involved in the biosynthesis of legionaminic acid, a virulence-associated, cell surface sialic acid-like derivative. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Glaze, P.A., Watson, D.C., Young, N.M. and Tanner, M.E. Biosynthesis of CMP-N,N′-diacetyllegionaminic acid from UDP-N,N′-diacetylbacillosamine in Legionella pneumophila. Biochemistry 47 (2008) 3272–3282. [DOI] [PMID: 18275154] |
2. |
Schoenhofen, I.C., Vinogradov, E., Whitfield, D.M., Brisson, J.R. and Logan, S.M. The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors. Glycobiology 19 (2009) 715–725. [DOI] [PMID: 19282391] |
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[EC 2.5.1.101 created 2012] |
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EC |
2.6.1.34 |
Accepted name: |
UDP-N-acetylbacillosamine transaminase |
Reaction: |
UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-α-D-xylo-hex-4-ulose + L-glutamate |
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For diagram of legionaminic acid biosynthesis, click here |
Glossary: |
UDP-N-acetylbacillosamine = UDP-2-acetamido-4-amino-2,4,6-trideoxy-α-D-glucose = UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine |
Other name(s): |
uridine diphospho-4-amino-2-acetamido-2,4,6-trideoxyglucose aminotransferase; UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine transaminase; UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase; pglE (gene name); UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose:2-oxoglutarate aminotransferase |
Systematic name: |
UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine:2-oxoglutarate aminotransferase |
Comments: |
A pyridoxal-phosphate protein. 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 [2-4] and O-linked glycosylation of certain L-serine residues in Neisseria species [5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-89-7 |
References: |
1. |
Distler, J., Kaufman, B. and Roseman, S. Enzymic synthesis of a diamino sugar nucleotide by extracts of type XIV Diplococcus pneumoniae. Arch. Biochem. Biophys. 116 (1966) 466–478. [DOI] [PMID: 4381351] |
2. |
Olivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B. In vitro biosynthesis of UDP-N,N′-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry 45 (2006) 13659–13669. [DOI] [PMID: 17087520] |
3. |
Schoenhofen, I.C., McNally, D.J., Vinogradov, E., Whitfield, D., Young, N.M., Dick, S., Wakarchuk, W.W., Brisson, J.R. and Logan, S.M. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. J. Biol. Chem. 281 (2006) 723–732. [DOI] [PMID: 16286454] |
4. |
Rangarajan, E.S., Ruane, K.M., Sulea, T., Watson, D.C., Proteau, A., Leclerc, S., Cygler, M., Matte, A. and Young, N.M. 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 (2008) 1827–1836. [DOI] [PMID: 18198901] |
5. |
Hartley, M.D., Morrison, M.J., Aas, F.E., Borud, B., Koomey, M. and Imperiali, B. Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N′-diacetylbacillosamine. Biochemistry 50 (2011) 4936–4948. [DOI] [PMID: 21542610] |
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[EC 2.6.1.34 created 1972, modified 2013] |
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EC
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2.6.1.91
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Deleted entry: | UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine transaminase. Identical to EC 2.6.1.34, UDP-N-acetylbacillosamine transaminase. |
[EC 2.6.1.91 created 2011, deleted 2013] |
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EC |
2.7.7.82 |
Accepted name: |
CMP-N,N′-diacetyllegionaminic acid synthase |
Reaction: |
CTP + N,N′-diacetyllegionaminate = CMP-N,N′-diacetyllegionaminate + diphosphate |
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For diagram of legionaminic acid biosynthesis, click here |
Glossary: |
legionaminate = 5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonate |
Other name(s): |
CMP-N,N′-diacetyllegionaminic acid synthetase; neuA (gene name); legF (gene name) |
Systematic name: |
CTP:N,N′-diacetyllegionaminate cytidylyltransferase |
Comments: |
Isolated from the bacteria Legionella pneumophila and Campylobacter jejuni. Involved in biosynthesis of legionaminic acid, a sialic acid-like derivative that is incorporated into virulence-associated cell surface glycoconjugates which may include lipopolysaccharide (LPS), capsular polysaccharide, pili and flagella. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Glaze, P.A., Watson, D.C., Young, N.M. and Tanner, M.E. Biosynthesis of CMP-N,N′-diacetyllegionaminic acid from UDP-N,N′-diacetylbacillosamine in Legionella pneumophila. Biochemistry 47 (2008) 3272–3282. [DOI] [PMID: 18275154] |
2. |
Schoenhofen, I.C., Vinogradov, E., Whitfield, D.M., Brisson, J.R. and Logan, S.M. The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors. Glycobiology 19 (2009) 715–725. [DOI] [PMID: 19282391] |
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[EC 2.7.7.82 created 2012] |
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EC |
2.7.8.36 |
Accepted name: |
undecaprenyl phosphate N,N′-diacetylbacillosamine 1-phosphate transferase |
Reaction: |
UDP-N,N′-diacetylbacillosamine + tritrans,heptacis-undecaprenyl phosphate = UMP + N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol |
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For diagram of undecaprenyldiphosphoheptasaccharide biosynthesis, click here |
Glossary: |
UDP-N,N′-diacetylbacillosamine = UDP-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose |
Other name(s): |
PglC |
Systematic name: |
UDP-N,N′-diacetylbacillosamine:tritrans,heptacis-undecaprenyl-phosphate N,N′-diacetylbacillosamine transferase |
Comments: |
Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Glover, K.J., Weerapana, E., Chen, M.M. and Imperiali, B. Direct biochemical evidence for the utilization of UDP-bacillosamine by PglC, an essential glycosyl-1-phosphate transferase in the Campylobacter jejuni N-linked glycosylation pathway. Biochemistry 45 (2006) 5343–5350. [DOI] [PMID: 16618123] |
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[EC 2.7.8.36 created 2012] |
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EC |
3.2.1.184 |
Accepted name: |
UDP-N,N′-diacetylbacillosamine 2-epimerase (hydrolysing) |
Reaction: |
UDP-N,N′-diacetylbacillosamine + H2O = UDP + 2,4-diacetamido-2,4,6-trideoxy-D-mannopyranose |
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For diagram of legionaminic acid biosynthesis, click here, and for mechanism, click here |
Glossary: |
UDP-N,N′-diacetylbacillosamine = UDP-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose |
Other name(s): |
UDP-Bac2Ac4Ac 2-epimerase; NeuC |
Systematic name: |
UDP-N,N′-diacetylbacillosamine hydrolase (2-epimerising) |
Comments: |
Requires Mg2+. Involved in biosynthesis of legionaminic acid, a nonulosonate derivative that is incorporated by some bacteria into assorted virulence-associated cell surface glycoconjugates. The initial product formed by the enzyme from Legionella pneumophila, which incorporates legionaminic acid into the O-antigen moiety of its lipopolysaccharide, is 2,4-diacetamido-2,4,6-trideoxy-α-D-mannopyranose, which rapidly mutarotates to a mixture of anomers [1]. The enzyme from Campylobacter jejuni, which incorporates legionaminic acid into flagellin, prefers GDP-N,N′-diacetylbacillosamine [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Glaze, P.A., Watson, D.C., Young, N.M. and Tanner, M.E. Biosynthesis of CMP-N,N′-diacetyllegionaminic acid from UDP-N,N′-diacetylbacillosamine in Legionella pneumophila. Biochemistry 47 (2008) 3272–3282. [DOI] [PMID: 18275154] |
2. |
Schoenhofen, I.C., Vinogradov, E., Whitfield, D.M., Brisson, J.R. and Logan, S.M. The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors. Glycobiology 19 (2009) 715–725. [DOI] [PMID: 19282391] |
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[EC 3.2.1.184 created 2012] |
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EC |
4.2.1.135 |
Accepted name: |
UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining) |
Reaction: |
UDP-N-acetyl-α-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-α-D-xylo-hex-4-ulose + H2O |
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For diagram of legionaminic acid biosynthesis, click here, and for mechanism, click here |
Glossary: |
N,N′-diacetylbacillosamine = 2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose |
Other name(s): |
PglF |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine hydro-lyase (configuration-retaining; UDP-2-acetamido-2,6-dideoxy-α-D-xylo-hex-4-ulose-forming) |
Comments: |
Contains NAD+ as a cofactor [2]. This is the first enzyme in the biosynthetic pathway of N,N′-diacetylbacillosamine [1], the first carbohydrate in the glycoprotein N-linked heptasaccharide in Campylobacter jejuni. This enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Schoenhofen, I.C., McNally, D.J., Vinogradov, E., Whitfield, D., Young, N.M., Dick, S., Wakarchuk, W.W., Brisson, J.R. and Logan, S.M. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. J. Biol. Chem. 281 (2006) 723–732. [DOI] [PMID: 16286454] |
2. |
Olivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B. In vitro biosynthesis of UDP-N,N′-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry 45 (2006) 13659–13669. [DOI] [PMID: 17087520] |
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[EC 4.2.1.135 created 2012] |
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