The Enzyme Database

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EC 2.3.1.203     
Accepted name: UDP-N-acetylbacillosamine N-acetyltransferase
Reaction: acetyl-CoA + UDP-N-acetylbacillosamine = CoA + UDP-N,N′-diacetylbacillosamine
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
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]
[EC 2.3.1.203 created 2012, modified 2013]
 
 
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
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]
[EC 2.5.1.101 created 2012]
 
 
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
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, 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]
[EC 2.6.1.34 created 1972, modified 2013]
 
 
EC 2.6.1.91      
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]
 
 
EC 2.7.7.82     
Accepted name: CMP-N,N′-diacetyllegionaminic acid synthase
Reaction: CTP + N,N′-diacetyllegionaminate = CMP-N,N′-diacetyllegionaminate + diphosphate
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]
[EC 2.7.7.82 created 2012]
 
 
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
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
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]
[EC 2.7.8.36 created 2012]
 
 
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
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
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]
[EC 3.2.1.184 created 2012]
 
 
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
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]
[EC 4.2.1.135 created 2012]
 
 


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