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Adenosine diphosphoglyceromannoheptose 6-epimerase
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ADP-glycero-manno-heptose-6-epimerase
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ADP-glyceromanno-heptose 6-epimerase
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ADP-L,D-hep 6-epimerase
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ADP-L-glycero-D-manno-heptose 6-epimerase
ADP-L-glycero-D-manno-heptose-6-epimerase
ADP-L-glycero-D-manno-heptose-epimerase, Aquifex aelicis gene rfaD
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ADP-L-glycero-D-mannoheptose 6-epimerase
ADP-L-glycero-D-mannoheptose 6-epimerase (Neisseria gonorrhoeae gene gme)
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ADP-L-glycero-D-mannoheptose-6-epimerase
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ADP-L-glycero-D-mannoheptose-6-epimerase (Escherichia coli strain K-12 substrain MG1655 clone EC19-98 gene rfaD)
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Epimerase, adenosine diphosphoglyceromannoheptose 6-
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Epimerase, adenosine diphosphoglyceromannoheptose 6- (Escherichia coli clone pCG50 reduced)
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Epimerase, adenosine diphosphoglyceromannoheptose 6- (Neisseria gonorrhoeae gene lis-6)
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Genbank AE000440-derived protein GI 1790049
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GenBank AE000684-derived protein GI 2983012
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ADP-L-glycero-D-manno-heptose 6-epimerase
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ADP-L-glycero-D-manno-heptose 6-epimerase
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ADP-L-glycero-D-manno-heptose 6-epimerase
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ADP-L-glycero-D-manno-heptose 6-epimerase
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ADP-L-glycero-D-manno-heptose-6-epimerase
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ADP-L-glycero-D-manno-heptose-6-epimerase
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ADP-L-glycero-D-manno-heptose-6-epimerase
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ADP-L-glycero-D-manno-heptose-6-epimerase
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ADP-L-glycero-D-manno-heptose-6-epimerase
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ADP-L-glycero-D-mannoheptose 6-epimerase
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ADP-L-glycero-D-mannoheptose 6-epimerase
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AGME
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HP0859
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RfaD
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ADP-beta-D-glycero-D-manno-heptose
ADP-beta-L-glycero-D-mannoheptose
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-
?
ADP-beta-D-manno-hexadialdose
ADP-beta-D-mannuronic acid + ADP-beta-D-mannose
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the intermediate ADP-beta-D-manno-hexadialdose undergoes dismutation into equal amounts of ADP-beta-D-mannuronic acid and ADP-beta-D-mannose
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?
ADP-D-glycero-D-manno-heptose
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
ADP-D-glycero-D-mannoheptose
ADP-L-glycero-D-mannoheptose
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?
ADP-D-glycero-D-manno-heptose
?
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the enzyme is required for lipopolysaccharide core biosynthesis
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?
ADP-D-glycero-D-manno-heptose
?
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the enzyme is involved in the biosynthesis of ADP-L-glycero-D-mannoheptose, which is a key intermediate of lipopolysaccharide inner core
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?
ADP-D-glycero-D-manno-heptose
?
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the enzyme is required for the biosynthesis of the lipopolysaccharide precursor ADP-L-glycero-D-manno-heptose
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?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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ADP-L-glycero-D-manno-heptose is a required intermediate for lipopolysaccharide inner-core and outer-membrane biosynthesis
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?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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direct C-6' oxidation/reduction mechanism
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?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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it is suggested that the mechanism involves transient oxidation directly at C-6'
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-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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mechanistic study, evidence for a direct oxidation mechanism in which the hydride initially transferred to the NADP+ cofactor is subsequently returned to the same carbon in a nonstereospecific manner
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?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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biosynthetic pathway of L-glycero-D-manno-heptose
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r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
?
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ADP-beta-D-glycero-D-manno-heptose
ADP-beta-L-glycero-D-mannoheptose
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-
-
-
?
ADP-D-glycero-D-manno-heptose
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
ADP-D-glycero-D-manno-heptose
?
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the enzyme is required for lipopolysaccharide core biosynthesis
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-
?
ADP-D-glycero-D-manno-heptose
?
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the enzyme is involved in the biosynthesis of ADP-L-glycero-D-mannoheptose, which is a key intermediate of lipopolysaccharide inner core
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-
?
ADP-D-glycero-D-manno-heptose
?
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the enzyme is required for the biosynthesis of the lipopolysaccharide precursor ADP-L-glycero-D-manno-heptose
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?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
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r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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ADP-L-glycero-D-manno-heptose is a required intermediate for lipopolysaccharide inner-core and outer-membrane biosynthesis
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?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
biosynthetic pathway of L-glycero-D-manno-heptose
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r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
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-
-
?
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malfunction
a HP0859 knockout mutant shows a severe loss of lipopolysaccharide structure and a significant reduction of adhesion levels in an infection model to human stomach gastric adenocarcinoma AGS cells, if compared with the wild-type strain
malfunction
the Escherichia coli rfaD-deletion mutant strain WJW00 can synthesize Kdo2-lipid A. 3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo)2-lipid A is the conserved structure domain of lipopolysaccharide found in most Gram-negative bacteria, and is believed to stimulate the human innate immune system through the TLR4/MD2 complex. Kdo2-lipid A is an important stimulator for studying the mechanism of the innate immune system and for developing bacterial vaccine adjuvants. Compared with the wild-type strain W3110, WJW00 shows increased hydrophobicity, higher cell permeability, greater autoaggregation and decreased biofilm-forming ability. Phenotypes, overview
malfunction
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a HP0859 knockout mutant shows a severe loss of lipopolysaccharide structure and a significant reduction of adhesion levels in an infection model to human stomach gastric adenocarcinoma AGS cells, if compared with the wild-type strain
-
malfunction
-
the Escherichia coli rfaD-deletion mutant strain WJW00 can synthesize Kdo2-lipid A. 3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo)2-lipid A is the conserved structure domain of lipopolysaccharide found in most Gram-negative bacteria, and is believed to stimulate the human innate immune system through the TLR4/MD2 complex. Kdo2-lipid A is an important stimulator for studying the mechanism of the innate immune system and for developing bacterial vaccine adjuvants. Compared with the wild-type strain W3110, WJW00 shows increased hydrophobicity, higher cell permeability, greater autoaggregation and decreased biofilm-forming ability. Phenotypes, overview
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metabolism
last enzyme in the pathway that produces L-glycero-D-manno-heptose starting from sedoheptulose-7-phosphate
metabolism
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last enzyme in the pathway that produces L-glycero-D-manno-heptose starting from sedoheptulose-7-phosphate
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additional information
an N-terminal seven-stranded modified Rossmann fold where the NAD+ cofactor is bound and a smaller C-terminal alpha/beta domain are responsible for the binding of the substrate
additional information
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an N-terminal seven-stranded modified Rossmann fold where the NAD+ cofactor is bound and a smaller C-terminal alpha/beta domain are responsible for the binding of the substrate
additional information
the enzyme contains a catalytic triad involved in catalyzing hydride transfer with the aid of NADP+. The enzyme may recognize their substrate in a lock-and-key fashion, binding analysis, docking study, enzyme structure comparisons, detailed overview
additional information
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the enzyme contains a catalytic triad involved in catalyzing hydride transfer with the aid of NADP+. The enzyme may recognize their substrate in a lock-and-key fashion, binding analysis, docking study, enzyme structure comparisons, detailed overview
additional information
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an N-terminal seven-stranded modified Rossmann fold where the NAD+ cofactor is bound and a smaller C-terminal alpha/beta domain are responsible for the binding of the substrate
-
additional information
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the enzyme contains a catalytic triad involved in catalyzing hydride transfer with the aid of NADP+. The enzyme may recognize their substrate in a lock-and-key fashion, binding analysis, docking study, enzyme structure comparisons, detailed overview
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purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing of 200 nl of 8.8 mg/ml protein in 0.43 M NaCl, 20 mM Tris-HCl, pH 8.0, with 200 nl of reservoir solution containing 35% PEG 200, 0.1 M bis-tris-HCl, pH 5.5, and equilibration against 0.05 ml of reservori solution, method optimization, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement
hanging-drop vapor-diffusion method, three crystal forms
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structure of the enzyme in complex with NADP+ and the inhibitor ADP-glucose, determined at 2.0 A resolution by multiwavelength anomalous diffraction phasing method
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Y140F mutant enzyme bound to ADP-beta-D-mannose, hanging drop vapor diffusion method, using 2M (NH4)2SO4, 0.1 M HEPES-Na, pH 7.1, 2% (w7v) PEG 400
purified recombinant His-tagged enzyme, vapor diffusion technique, mixing of 20 mg/ml protein in 30 mM Tris, pH 7.5, 150 mM NaCl, with precipitant solution containing 0.2 M ammonium sulfate, 0.1 M tri sodium citrate, pH 5.6, 15% w/v PEG 4000, and 5% glycerol, 20°C, X-ray diffraction structure determination and analysis at 2.55 A resolution
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E210G
site-directed mutagenesis, structure compared to the wild-type enzyme
K178M
site-directed mutagenesis, structure compared to the wild-type enzyme
E210G
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site-directed mutagenesis, structure compared to the wild-type enzyme
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K178M
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site-directed mutagenesis, structure compared to the wild-type enzyme
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D210N
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mutant display activity similar to that of the wild type
K178M
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mutant has severely compromised epimerase activities that are more than 3 orders of magnitude lower than that of the wild type
K208M
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mutant display activity similar to that of the wild type
Y140F
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mutant has severely compromised epimerase activities that are more than 3 orders of magnitude lower than that of the wild type
Y140F
the mutant shows 0.08% epimerase activity compared to the wild type enzyme
additional information
construction of the mutant Escherichia coli strains WBB06 and WJW00, that can synthesize Kdo2-lipid A, by deleting the rfaD gene from the genome of Escherichia coli wild-type strain W3110. 3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo)2-lipid A is the conserved structure domain of lipopolysaccharide found in most Gram-negative bacteria, and is believed to stimulate the human innate immune system through the TLR4/MD2 complex. Kdo2-lipid A is an important stimulator for studying the mechanism of the innate immune system and for developing bacterial vaccine adjuvants. Compared with the wild-type strain W3110, WJW00 shows increased hydrophobicity, higher cell permeability, greater autoaggregation and decreased biofilm-forming ability
additional information
-
construction of the mutant Escherichia coli strains WBB06 and WJW00, that can synthesize Kdo2-lipid A, by deleting the rfaD gene from the genome of Escherichia coli wild-type strain W3110. 3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo)2-lipid A is the conserved structure domain of lipopolysaccharide found in most Gram-negative bacteria, and is believed to stimulate the human innate immune system through the TLR4/MD2 complex. Kdo2-lipid A is an important stimulator for studying the mechanism of the innate immune system and for developing bacterial vaccine adjuvants. Compared with the wild-type strain W3110, WJW00 shows increased hydrophobicity, higher cell permeability, greater autoaggregation and decreased biofilm-forming ability
additional information
-
construction of the mutant Escherichia coli strains WBB06 and WJW00, that can synthesize Kdo2-lipid A, by deleting the rfaD gene from the genome of Escherichia coli wild-type strain W3110. 3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo)2-lipid A is the conserved structure domain of lipopolysaccharide found in most Gram-negative bacteria, and is believed to stimulate the human innate immune system through the TLR4/MD2 complex. Kdo2-lipid A is an important stimulator for studying the mechanism of the innate immune system and for developing bacterial vaccine adjuvants. Compared with the wild-type strain W3110, WJW00 shows increased hydrophobicity, higher cell permeability, greater autoaggregation and decreased biofilm-forming ability
-
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Pegues, J.C.; Chen, L.; Gordon, A.W.; Ding, L.; Coleman, W.G.
Cloning, expression, and characterization of the Escherichia coli K-12 rfaD gene
J. Bacteriol.
172
4652-4660
1990
Escherichia coli
brenda
Coleman, W.G.
The rfaD gene codes for ADP-L-glycero-D-mannoheptose-6-epimerase
J. Biol. Chem.
258
1985-1990
1983
Escherichia coli
brenda
Ding, L.; Seto, B.L.; Ahmed, S.A.; Coleman, W.G.
Purification and properties of the Escherichia coli K-12 NAD-dependent nucleotide diphosphosulfate epimerase, ADP-L-glycero-D-mannoheptose 6-epimerase
J. Biol. Chem.
269
24384-24390
1994
Escherichia coli
brenda
Drazek, E.S.; Stein, D.C.; Deal, C.D.
A mutation in the Neisseria gonorrhoeae rfaD homolog results in altered lipooligosaccharide expression
J. Bacteriol.
177
2321-2327
1995
Neisseria gonorrhoeae
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, Haemophilus influenzae 2019
brenda
Sirisena, D.M.; MacLachlan, P.R.; Liu, S.L.; Hessel, A.; Sanderson, K.E.
Molecular analysis of the rfaD gene, for heptose synthesis, and the rfaF gene, for heptose transfer, in lipopolysaccharide synthesis in Salmonella typhimurium
J. Bacteriol.
176
2379-2385
1994
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Ding, L.; Zhang, Y.; Deacon, A.M.; Ealick, S.E.; Ni, Y.; Sun, P.; Coleman, W.G., Jr.
Crystallization and preliminary X-ray diffraction studies of the lipopolysaccharide core biosynthetic enzyme ADP-L-glycero-D-mannoheptose 6-epimerase from Escherichia coli K-12
Acta Crystallogr. Sect. D
55
685-688
1999
Escherichia coli
brenda
Ni, Y.; McPhie, P.; Deacon, A.; Ealick, S.; Coleman, W.G., Jr.
Evidence that NADP+ is the physiological cofactor of ADP-L-glycero-D-mannoheptose 6-epimerase
J. Biol. Chem.
276
27329-27334
2001
Escherichia coli (P67910)
brenda
Deacon, A.M.; Ni, Y.S.; Coleman, W.G., Jr.; Ealick, S.E.
The crystal structure of ADP-L-glycero-D-mannoheptose 6-epimerase: catalysis with a twist
Structure
8
453-462
2000
Escherichia coli
brenda
Morrison, J.P.; Read, J.A.; Coleman, W.G., Jr.; Tanner, M.E.
Dismutase activity of ADP-L-glycero-D-manno-heptose 6-epimerase: evidence for a direct oxidation/reduction mechanism
Biochemistry
44
5907-5915
2005
Escherichia coli
brenda
Read, J.A.; Ahmed, R.A.; Morrison, J.P.; Coleman, W.G., Jr.; Tanner, M.E.
The mechanism of the reaction catalyzed by ADP-beta-L-glycero-D-manno-heptose 6-epimerase
J. Am. Chem. Soc.
126
8878-8879
2004
Escherichia coli
brenda
Read, J.A.; Ahmed, R.A.; Tanner, M.E.
Efficient chemoenzymatic synthesis of ADP-D-glycero-beta-D-manno-heptose and a mechanistic study of ADP-L-glycero-D-manno-heptose 6-epimerase
Org. Lett.
7
2457-2460
2005
Escherichia coli
brenda
Morrison, J.P.; Tanner, M.E.
A Two-Base Mechanism for Escherichia coli ADP-L-glycero-D-manno-Heptose 6-Epimerase
Biochemistry
46
3916-3924
2007
Escherichia coli
brenda
Mayer, A.; Tanner, M.E.
Intermediate release by ADP-L-glycero-D-manno-heptose 6-epimerase
Biochemistry
46
6149-6155
2007
Escherichia coli
brenda
Kim, H.; Lee, M.; Chun, S.; Park, S.; Lee, K.
Role of NtrC in biofilm formation via controlling expression of the gene encoding an ADP-glycero-manno-heptose-6-epimerase in the pathogenic bacterium, Vibrio vulnificus
Mol. Microbiol.
63
559-574
2007
Vibrio vulnificus
brenda
Kowatz, T.; Morrison, J.P.; Tanner, M.E.; Naismith, J.H.
The crystal structure of the Y140F mutant of ADP-L-glycero-D-manno-heptose 6-epimerase bound to ADP-beta-D-mannose suggests a one base mechanism
Protein Sci.
19
1337-1343
2010
Escherichia coli (P67910)
brenda
Kim, M.; Lim, A.; Yang, S.; Park, J.; Lee, D.; Shin, D.
Structure and in silico substrate-binding mode of ADP-L-glycero-D-manno-heptose 6-epimerase from Burkholderia thailandensis
Acta Crystallogr. Sect. D
69
658-668
2013
Burkholderia thailandensis (Q2SY18), Burkholderia thailandensis, Burkholderia thailandensis E444 (Q2SY18)
brenda
Shaik, M.M.; Zanotti, G.; Cendron, L.
The crystal structure of ADP-L-glycero-D-manno-heptose-6-epimerase (HP0859) from Helicobacter pylori
Biochim. Biophys. Acta
1814
1641-1647
2011
Helicobacter pylori (B5Z7L9), Helicobacter pylori, Helicobacter pylori G27 (B5Z7L9)
brenda
Wang, J.; Ma, W.; Wang, Z.; Li, Y.; Wang, X.
Construction and characterization of an Escherichia coli mutant producing Kdo2-lipid A
Mar. Drugs
12
1495-1511
2014
Escherichia coli (P67910), Escherichia coli, Escherichia coli W3110 / K-12 (P67910)
brenda