Any feedback?
Information on EC 5.1.3.20 - ADP-glyceromanno-heptose 6-epimerase
for references in articles please use BRENDA:EC5.1.3.20Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
5.1.3.20 ADP-glyceromanno-heptose 6-epimeraseIUBMB Comments
Requires NAD+.
Specify your search results
Word Map
- 5.1.3.20
- lipopolysaccharide
- nadp+
- lps
-
nonstereospecific
-
hydride
- udp-galactose
-
haemophilus
-
4-epimerase
-
coleman
-
heptosyltransferase
-
dismutation
-
epimerization
- novobiocin
-
non-pathogenic
-
epimeric
-
biofilm-forming
The enzyme appears in viruses and cellular organisms
Synonyms
hp0859, adp-l-glycero-d-mannoheptose-6-epimerase, adp-l-glycero-d-manno-heptose 6-epimerase, adp-l-glycero-d-mannoheptose 6-epimerase, adp-l-glycero-d-manno-heptose-6-epimerase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Adenosine diphosphoglyceromannoheptose 6-epimerase
-
-
-
-
ADP-glyceromanno-heptose 6-epimerase
-
-
-
-
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
-
-
-
-
ADP-L-glycero-D-mannoheptose 6-epimerase
ADP-L-glycero-D-mannoheptose 6-epimerase (Neisseria gonorrhoeae gene gme)
-
-
-
-
ADP-L-glycero-D-mannoheptose-6-epimerase
-
-
-
-
ADP-L-glycero-D-mannoheptose-6-epimerase (Escherichia coli strain K-12 substrain MG1655 clone EC19-98 gene rfaD)
-
-
-
-
AGME
Epimerase, adenosine diphosphoglyceromannoheptose 6-
-
-
-
-
Epimerase, adenosine diphosphoglyceromannoheptose 6- (Escherichia coli clone pCG50 reduced)
-
-
-
-
Epimerase, adenosine diphosphoglyceromannoheptose 6- (Neisseria gonorrhoeae gene lis-6)
-
-
-
-
Genbank AE000440-derived protein GI 1790049
-
-
-
-
GenBank AE000684-derived protein GI 2983012
-
-
-
-
HP0859
RfaD
ADP-L-glycero-D-manno-heptose-6-epimerase
-
-
-
-
ADP-L-glycero-D-mannoheptose 6-epimerase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ADP-D-glycero-D-manno-heptose = ADP-L-glycero-D-manno-heptose
-
-
-
-
ADP-D-glycero-D-manno-heptose = ADP-L-glycero-D-manno-heptose
catalytic one-base reaction mechanism from docking study, overview. The key point in the catalytic process of AGME is the inversion at the C6'' stereocentre of ADP-D,D-Hep mediated by the reversible redox reactions of NADP+/NADPH
ADP-D-glycero-D-manno-heptose = ADP-L-glycero-D-manno-heptose
catalytic one-base reaction mechanism from docking study, overview. The key point in the catalytic process of AGME is the inversion at the C6'' stereocentre of ADP-D,D-Hep mediated by the reversible redox reactions of NADP+/NADPH
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
epimerization
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ADP-L-glycero-D-manno-heptose 6-epimerase
Requires NAD+.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
130527-81-0
epimerase, adenosine diphosphoglyceromannoheptose 6- (Escherichia coli clone pCG50 reduced) /ADP-L-glycero-D-mannoheptose-6-epimerase (Escherichia coli strain K-12 substrain MG1655 clone EC19-98 gene rfaD) /genBank AE000440-derived protein GI 1790049
167617-20-1
epimerase, adenosine diphosphoglyceromannoheptose 6- (Neisseria gonorrhoeae gene lis-6), ADP-L-glycero-D-mannoheptose 6-epimerase (Neisseria gonorrhoeae gene gme)
204790-62-5
ADP-L-glycero-D-manno-heptose-epimerase, Aquifex aelicis gene rfaD /GenBank AE000684-derived protein GI 2983012
85030-75-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP-beta-D-glycero-D-manno-heptose
ADP-beta-L-glycero-D-mannoheptose
-
-
-
-
?
ADP-beta-D-manno-hexadialdose
ADP-beta-D-mannuronic acid + ADP-beta-D-mannose
-
the intermediate ADP-beta-D-manno-hexadialdose undergoes dismutation into equal amounts of ADP-beta-D-mannuronic acid and ADP-beta-D-mannose
-
-
?
ADP-D-glycero-D-manno-heptose
?
-
the enzyme is required for lipopolysaccharide core biosynthesis
-
-
?
ADP-D-glycero-D-manno-heptose
?
-
the enzyme is involved in the biosynthesis of ADP-L-glycero-D-mannoheptose, which is a key intermediate of lipopolysaccharide inner core
-
-
?
ADP-D-glycero-D-manno-heptose
?
-
the enzyme is required for the biosynthesis of the lipopolysaccharide precursor ADP-L-glycero-D-manno-heptose
-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
-
-
r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
-
-
r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
ADP-L-glycero-D-manno-heptose is a required intermediate for lipopolysaccharide inner-core and outer-membrane biosynthesis
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
direct C-6' oxidation/reduction mechanism
-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
it is suggested that the mechanism involves transient oxidation directly at C-6'
-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
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
-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
biosynthetic pathway of L-glycero-D-manno-heptose
-
-
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
-
-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP-beta-D-glycero-D-manno-heptose
ADP-beta-L-glycero-D-mannoheptose
-
-
-
-
?
ADP-D-glycero-D-manno-heptose
?
-
the enzyme is required for lipopolysaccharide core biosynthesis
-
-
?
ADP-D-glycero-D-manno-heptose
?
-
the enzyme is involved in the biosynthesis of ADP-L-glycero-D-mannoheptose, which is a key intermediate of lipopolysaccharide inner core
-
-
?
ADP-D-glycero-D-manno-heptose
?
-
the enzyme is required for the biosynthesis of the lipopolysaccharide precursor ADP-L-glycero-D-manno-heptose
-
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
-
-
r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
-
-
r
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
ADP-L-glycero-D-manno-heptose is a required intermediate for lipopolysaccharide inner-core and outer-membrane biosynthesis
-
?
ADP-D-glycero-D-manno-heptose
ADP-L-glycero-D-manno-heptose
-
biosynthetic pathway of L-glycero-D-manno-heptose
-
-
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
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
AGME preferentially utilizes NADP+ but can use NAD+ (lower activity)
NAD+
preferred cofactor compared to NADP+, binds at the enzyme active site, binding site structure, overview
NADP+
-
a large N-terminal domain consists of a modified seven-stranded Rossmann fold that is associated with NADP+ binding
NADP+
-
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
NADP+
the enzyme contains a catalytic triad involved in catalyzing hydride transfer with the aid of NADP+
additional information
preference of the enzyme for NAD+ compared to NADP+. When NADP is bound, the binding region assumes a different conformation
-
additional information
-
preference of the enzyme for NAD+ compared to NADP+. When NADP is bound, the binding region assumes a different conformation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
The crystal structure of ADP-L-glycero-D-manno-heptose-6-epimerase (HP0859) from Helicobacter pylori.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 55
-
5°C: about 45% of maximal activity, 55°C: about 50% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
additional information
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
-
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
Escherichia coli W3110 / K-12
-
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
-
metabolism
last enzyme in the pathway that produces L-glycero-D-manno-heptose starting from sedoheptulose-7-phosphate
metabolism
-
last enzyme in the pathway that produces L-glycero-D-manno-heptose starting from sedoheptulose-7-phosphate
-
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
-
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
-
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
-
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
-
Show AA Sequence and Transmembrane Helices (8796 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentamer
additional information
pentamer
structure modeling of the pentameric enzyme including five protein monomers and 5 NAD+ molecules, overview
pentamer
-
structure modeling of the pentameric enzyme including five protein monomers and 5 NAD+ molecules, overview
-
additional information
enzyme structure comparisons, detailed overview
additional information
-
enzyme structure comparisons, detailed overview
additional information
-
enzyme structure comparisons, detailed overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E210G
site-directed mutagenesis, structure compared to the wild-type enzyme
K178M
site-directed mutagenesis, structure compared to the wild-type enzyme
E210G
-
site-directed mutagenesis, structure compared to the wild-type enzyme
-
K178M
-
site-directed mutagenesis, structure compared to the wild-type enzyme
-
K178M
-
mutant has severely compromised epimerase activities that are more than 3 orders of magnitude lower than that of the wild type
Y140F
additional information
Y140F
-
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
Escherichia coli W3110 / K-12
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
metal affinity column chromatography, hydrophobic affinity column chromatography, and gel filtration
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gell filtration
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene HP0859, expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene rfaD, sequence compariosns, expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
identification of colicin E1 hybrid plasmid carrying the coding sequence for ADP-L-glycero-D-mannoheptose-6-epimerase from Clarke-carbon bank
-
Plasmids encoding hexahistidine-tagged mutant and wildtype enzymes overexpressed in Escherichia coli.
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.