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ADP-alpha-D-mannose + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
? + ADP
the enzyme is also able to utilize this nonphysiological donor substrate ADP-mannose although with less efficiency than with the natural substrate ADP-L-glycero-beta-D-manno-heptose
-
-
?
ADP-L-glycero-beta-D-manno-heptose + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->3)-alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
-
-
-
?
ADP-L-glycero-beta-D-manno-heptose + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->3)-alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
-
-
-
?
ADP-L-glycero-beta-D-manno-heptose + Kdo2-lipid A
ADP + Hep2-Kdo2-lipid A
ADP-L-glycero-beta-D-manno-heptose + Kdo2-lipid A
ADP + Hep2-Kdo2-lipid A
-
-
-
?
ADP-L-glycero-beta-D-manno-heptose + Kdo2-lipid A
ADP + Hep2-Kdo2-lipid A
-
-
-
?
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malfunction
deletion of the enzyme's gene disables the flagella biosynthesis in Escherichia coli
malfunction
-
enzyme inactivation leads to truncation of lipooligosaccharides core oligosaccharides, increased surface hydrophobicity and decreased numbers of cells attaching to stainless steel and glass
malfunction
-
enzyme inactivation leads to truncation of lipooligosaccharides core oligosaccharides, increased surface hydrophobicity and decreased numbers of cells attaching to stainless steel and glass
malfunction
inactivation of the Haemophilus ducreyi waaF gene by insertion mutagenesis results in expression of a lipooligosaccharide that migrates much faster than wild-type lipooligosaccharide in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The lipooligosaccharide of this mutant does not bind a monoclonal antibody directed against a cell surface-exposed epitope of wild-type Haemophilus ducreyi lipooligosaccharide. This waaF mutant is less virulent than the wild-type parent strain
malfunction
-
deletion of the enzyme's gene disables the flagella biosynthesis in Escherichia coli
-
malfunction
-
inactivation of the Haemophilus ducreyi waaF gene by insertion mutagenesis results in expression of a lipooligosaccharide that migrates much faster than wild-type lipooligosaccharide in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The lipooligosaccharide of this mutant does not bind a monoclonal antibody directed against a cell surface-exposed epitope of wild-type Haemophilus ducreyi lipooligosaccharide. This waaF mutant is less virulent than the wild-type parent strain
-
physiological function
the enzyme is involved in virulence expression
physiological function
the loss of heptosyltransferase activity results in the production of a truncated core oligosaccharide, failure to bind specific ligands, and loss of serum reactive GM1, asialo-GM1, and GM2 ganglioside epitopes. The mutation of waaF does not affect the higher-molecular-weight polysaccharide supporting the production of a LOS-independent capsular polysaccharide by Campylobacter jejuni
physiological function
-
the loss of heptosyltransferase activity results in the production of a truncated core oligosaccharide, failure to bind specific ligands, and loss of serum reactive GM1, asialo-GM1, and GM2 ganglioside epitopes. The mutation of waaF does not affect the higher-molecular-weight polysaccharide supporting the production of a LOS-independent capsular polysaccharide by Campylobacter jejuni
-
physiological function
-
the enzyme is involved in virulence expression
-
physiological function
-
the loss of heptosyltransferase activity results in the production of a truncated core oligosaccharide, failure to bind specific ligands, and loss of serum reactive GM1, asialo-GM1, and GM2 ganglioside epitopes. The mutation of waaF does not affect the higher-molecular-weight polysaccharide supporting the production of a LOS-independent capsular polysaccharide by Campylobacter jejuni
-
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Gronow, S.; Brabetz, W.; Brade, H.
Comparative functional characterization in vitro of heptosyltransferase I (WaaC) and II (WaaF) from Escherichia coli
Eur. J. Biochem.
267
6602-6611
2000
Escherichia coli (P37692), Escherichia coli
brenda
Gronow, S.; Oertelt, C.; Ervel, E.; Zamyatina, A.; Kosma, P.; Skurnik, M.; Holst, O.
Characterization of the physiological substrate for lipopolysaccharide heptosyltransferases I and II
J. Endotoxin Res.
7
263-270
2001
Escherichia coli (P37692)
brenda
Wang, Z.; Wang, J.; Ren, G.; Li, Y.; Wang, X.
Deletion of the genes waaC, waaF, or waaG in Escherichia coli W3110 disables the flagella biosynthesis
J. Basic Microbiol.
56
1021-1035
2016
Escherichia coli (P37692), Escherichia coli W3110 / ATCC 27325 (P37692)
brenda
Nguyen, V.T.; Barlow, R.S.; Fegan, N.; Turner, M.S.; Dykes, G.A.
Role of capsular polysaccharides and lipooligosaccharides in Campylobacter surface properties, autoagglutination, and attachment to abiotic surfaces
Foodborne Pathog. Dis.
10
506-513
2013
Campylobacter jejuni, Escherichia coli
brenda
Nichols, W.A.; Gibson, B.W.; Melaugh, W.; Lee, N.G.; Sunshine, M.; Apicella, M.A.
Identification of the ADP-L-glycero-D-manno-heptose-6-epimerase (rfaD) and heptosyltransferase II (rfaF) biosynthesis genes from nontypeable Haemophilus influenzae 2019
Infect. Immun.
65
1377-1386
1997
Haemophilus influenzae (Q48229), Haemophilus influenzae, Haemophilus influenzae 2019 (Q48229), Haemophilus influenzae 2019
brenda
Bauer, B.; Lumbley, S.; Hansen, E.
Characterization of a WaaF (RfaF) homolog expressed by Haemophilus ducreyi
Infect. Immun.
67
899-907
1999
[Haemophilus] ducreyi (Q7VNA4), [Haemophilus] ducreyi 35000HP (Q7VNA4)
brenda
De Kievit, T.; Lam, J.
Isolation and characterization of two genes, waaC (rfaC) and waaF (rfaF), involved in Pseudomonas aeruginosa serotype 05 inner-core biosynthesis
J. Bacteriol.
179
3451-3457
1997
Pseudomonas aeruginosa (O05196)
brenda
Allen, A.; Isobe, T.; Maskell, D.
Identification and cloning of waaF (rfaF) from Bordetella pertussis and use to generate mutants of Bordetella spp. with deep rough lipopolysaccharide
J. Bacteriol.
180
35-40
1998
Bordetella pertussis (O07076), Bordetella pertussis
brenda
Oldfield, N.J.; Moran, A.P.; Millar, L.A.; Prendergast, M.M.; Ketley, J.M.
Characterization of the Campylobacter jejuni heptosyltransferase II gene, waaF, provides genetic evidence that extracellular polysaccharide is lipid A core independent
J. Bacteriol.
184
2100-2107
2002
Campylobacter jejuni, Campylobacter jejuni (Q0P9A8), Campylobacter jejuni NCTC 11168 (Q0P9A8), Campylobacter jejuni NCTC 11828
brenda