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2 UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + 2 H2O
UDP-6-deoxy-6-fluoro-GlcNAc
UDP-GlcNAc + HF
-
elimination of fluoride from the substrate by the wild-type PseB, no activity by mutant enzymes K127A, D126N, and Y135F
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-
?
UDP-GlcNAc
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hexos-4-ulose + H2O
UDP-N-acetyl-alpha-D-glucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
additional information
?
-
2 UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + 2 H2O
-
the Cj1293 enzyme exhibits C6 dehydratase as well as C5 epimerase activity resulting in the production of both UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose. The enzyme is involved in biosynthesis of pseudaminic acid for glycomodification of the bacterial falgellins, overview
NMR analysis of reaction products, overview
-
?
2 UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + 2 H2O
-
the Cj1293 enzyme exhibits C6 dehydratase as well as C5 epimerase activity resulting in the production of both UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose. The enzyme is involved in biosynthesis of pseudaminic acid for glycomodification of the bacterial falgellins, overview
NMR analysis of reaction products, overview
-
?
2 UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + 2 H2O
-
the HP0840 enzyme exhibits C6 dehydratase as well as C5 epimerase activity resulting in the production of both UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose. The enzyme is involved in biosynthesis of pseudaminic acid for glycomodification of the bacterial falgellins, overview
NMR analysis of reaction products, overview
-
?
UDP-GlcNAc
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hexos-4-ulose + H2O
-
the enzyme is involved in the pseudaminic acid biosynthesis, it is responsible for the biosynthesis of 6-deoxyhexose
-
-
?
UDP-GlcNAc
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hexos-4-ulose + H2O
-
the C-5'' epimerization of UDP-4-keto-6-deoxy-L-IdoNAc to UDP-4-keto-6-deoxy-GlcNAc is PseB-catalyzed, and is about 50fold lower than the dehydratase activity
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?
UDP-N-acetyl-alpha-D-glucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
CapE is a 5-inverting 4,6-dehydratase enzyme, but in the absence of downstream enzymes, CapE catalyzes an additional reaction (5-back-epimerization) affording a by-product UDP-xylo-sugar under thermodynamic control. The by-product structural analysis reveals a network of coordinated motions away from the active site governing the enzymatic activity of CapE. A second dynamic element (the latch) regulates the enzymatic chemoselectivity, second molecule of UDP-sugar is found at another binding pocket remote from the active site. The secondary binding site stabilizes the conformation of the latch and may play a role in the enzymatic regulation of CapE as observed in other enzymes. The by-product is anchored to the protein by non-covalent interactions through its UDP moiety
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?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
-
-
-
?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
production of a precursor of pseudaminic acid, i.e. 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno-nonulosonic acid, required for flagellin glycosylation in Helicobacter pylori, analysis of all reaction steps in the pathway and related enzymes, overview
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?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
the enzyme catalyzes the first step in the biosynthetic pathway of a pseudaminic acid derivative, which is implicated in protein glycosylation
-
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?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
the enzyme is required for pseudaminic acid biosynthesis, which is required for O-linked flagellin glycosylation
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?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
NMR reaction analysis, a possible three-step reaction mechanism that involves Lys133 functioning as both a catalytic acid and base
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?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
NMR reaction analysis, substrate binding at the active site, mapping of dynamic interactions of the enzyme with its ligand, molecular docking, overview
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?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
the enzyme catalyzes the stereospecific conversion of UDP-GlcNAc to Qui2NAc, i.e. 2-acetamido-2,6-dideoxy-D-glucose or N-acetylquinovosamine, via the formation of a 4-keto, 6-deoxy intermediate
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?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
WbpM is specific for UDP-GlcNAc
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?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
WbpM is specific for UDP-GlcNAc. Although WbpM possesses an altered catalytic triad composed of SMK as opposed to SYK commonly found in other dehydratases, its catalysis is very efficient
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?
additional information
?
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the flagellar aminotransferases Cj1294 utilize only UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose as substrate producing UDP-4-amino-4,6-dideoxy-beta-L-AltNAc, a precursor in the Pse biosynthetic pathway
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?
additional information
?
-
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the flagellar aminotransferases Cj1294 utilize only UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose as substrate producing UDP-4-amino-4,6-dideoxy-beta-L-AltNAc, a precursor in the Pse biosynthetic pathway
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?
additional information
?
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dependence of O-linked flagellin glycosylation on PseB, cross-talk between the Pse and alpha-D-QuiNAc4NAc, i.e. 2,4-diacetamido-2,4,6-trideoxy-a-d-Glc, pathways via PseB
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?
additional information
?
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the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in lipopolysaccharide and flagellum production with glycosylation regulating the activity of these proteins
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?
additional information
?
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in lipopolysaccharide and flagellum production with glycosylation regulating the activity of these proteins
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?
additional information
?
-
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in lipopolysaccharide and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in LPS and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in LPS and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in LPS and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
-
the flagellar aminotransferases HP0366 utilize only UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose as substrate producing UDP-4-amino-4,6-dideoxy-beta-L-AltNAc, a precursor in the Pse biosynthetic pathway
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?
additional information
?
-
-
FlaA1 is a bifunctional C6 dehydratase/C4 reductase specific for UDPGlcNAc. It converts UDP-GlcNAc into a UDP-4-keto-6-methyl-GlcNAc intermediate, which is stereospecifically reduced into UDP-QuiNAc
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?
additional information
?
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no activity with UDP-Glc, UDP-Gal, or UDP-GalNAc or with substrates of other known C6 dehydratases, i.e. GDP-mannose or dTDP-glucose, structure-function analysis, overview
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?
additional information
?
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PseB catalyzes an additional C5 epimerization forming UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hexos-4-ulose
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?
additional information
?
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in lipopolysaccharide and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in LPS and flagellum production with glycosylation regulating the activity of these proteins
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-
?
additional information
?
-
purified Mg534 protein is incubated in 50 mM Tris-HCl, 150 mM NaCl, pH 7.5, 25°C, in the presence of 0.2 mM UDP-GlcNAc and 0.1 mM NADP+, GC-MS product identification and analysis
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?
additional information
?
-
WbpM is essential for the biosynthesis of B-band lipopolysaccharide in many serotypes of Pseudomonas aeruginosa
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?
additional information
?
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WbpM is essential for the biosynthesis of B-band lipopolysaccharide in many serotypes of Pseudomonas aeruginosa
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?
additional information
?
-
no activity with UDP-Glc, UDP-GalNAc or UDP-Gal, and with substrates of other known C6 dehydratases such as GDP-mannose, dTDP-Glc and CDP-Glc. Structure-function analysis, although the membrane domains do not have any catalytic activity, they are important for the polymerization of high-molecular weight B-band lipopolysaccharide, overview
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?
additional information
?
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-
no activity with UDP-Glc, UDP-GalNAc or UDP-Gal, and with substrates of other known C6 dehydratases such as GDP-mannose, dTDP-Glc and CDP-Glc. Structure-function analysis, although the membrane domains do not have any catalytic activity, they are important for the polymerization of high-molecular weight B-band lipopolysaccharide, overview
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + 2 H2O
UDP-GlcNAc
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hexos-4-ulose + H2O
-
the enzyme is involved in the pseudaminic acid biosynthesis, it is responsible for the biosynthesis of 6-deoxyhexose
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-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
additional information
?
-
2 UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + 2 H2O
-
the Cj1293 enzyme exhibits C6 dehydratase as well as C5 epimerase activity resulting in the production of both UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose. The enzyme is involved in biosynthesis of pseudaminic acid for glycomodification of the bacterial falgellins, overview
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-
?
2 UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + 2 H2O
-
the Cj1293 enzyme exhibits C6 dehydratase as well as C5 epimerase activity resulting in the production of both UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose. The enzyme is involved in biosynthesis of pseudaminic acid for glycomodification of the bacterial falgellins, overview
-
-
?
2 UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + 2 H2O
-
the HP0840 enzyme exhibits C6 dehydratase as well as C5 epimerase activity resulting in the production of both UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose. The enzyme is involved in biosynthesis of pseudaminic acid for glycomodification of the bacterial falgellins, overview
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-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
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-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
-
-
?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
-
-
-
?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
production of a precursor of pseudaminic acid, i.e. 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno-nonulosonic acid, required for flagellin glycosylation in Helicobacter pylori, analysis of all reaction steps in the pathway and related enzymes, overview
-
-
?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
the enzyme catalyzes the first step in the biosynthetic pathway of a pseudaminic acid derivative, which is implicated in protein glycosylation
-
-
?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
-
the enzyme is required for pseudaminic acid biosynthesis, which is required for O-linked flagellin glycosylation
-
-
?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
WbpM is specific for UDP-GlcNAc
-
-
?
additional information
?
-
-
the flagellar aminotransferases Cj1294 utilize only UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose as substrate producing UDP-4-amino-4,6-dideoxy-beta-L-AltNAc, a precursor in the Pse biosynthetic pathway
-
-
?
additional information
?
-
-
the flagellar aminotransferases Cj1294 utilize only UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose as substrate producing UDP-4-amino-4,6-dideoxy-beta-L-AltNAc, a precursor in the Pse biosynthetic pathway
-
-
?
additional information
?
-
-
dependence of O-linked flagellin glycosylation on PseB, cross-talk between the Pse and alpha-D-QuiNAc4NAc, i.e. 2,4-diacetamido-2,4,6-trideoxy-a-d-Glc, pathways via PseB
-
-
?
additional information
?
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in lipopolysaccharide and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in lipopolysaccharide and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in lipopolysaccharide and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in LPS and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in LPS and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in LPS and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
-
the flagellar aminotransferases HP0366 utilize only UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose as substrate producing UDP-4-amino-4,6-dideoxy-beta-L-AltNAc, a precursor in the Pse biosynthetic pathway
-
-
?
additional information
?
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in lipopolysaccharide and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
the enzyme is involved in lipopolysaccharide biosynthesis, flagellum assembly, or protein glycosylation, and might play an important role in the pathogenesis of Helicobacter pylori. It is at the interface between several pathways that govern the expression of different virulence factors synthesizing sugar derivatives dedicated to the glycosylation of proteins which are involved in LPS and flagellum production with glycosylation regulating the activity of these proteins
-
-
?
additional information
?
-
WbpM is essential for the biosynthesis of B-band lipopolysaccharide in many serotypes of Pseudomonas aeruginosa
-
-
?
additional information
?
-
-
WbpM is essential for the biosynthesis of B-band lipopolysaccharide in many serotypes of Pseudomonas aeruginosa
-
-
?
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additional information
two different types of enzymes are identified. In one case, this step is a simple dehydration with formation of UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose, which is typical of the UDP-bacillosamine or UDP-N-acetyl-D-fucosamine and UDP-N-acetyl-D-quinovosamine pathways. In other cases, the enzymes are inverting 4,6-dehydratases, catalyzing also the epimerization of C-5, with the consequent inversion of the D-configuration to L-, and the formation of UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose. This reaction is catalyzed by PseB/FlaA1 in the case of the pseudaminic acid (Pse) pathway, where the transfer of an amino group to the C-4 carbonyl follows this first step. Superposition of the NADPH binding domain of Mg534 with CapE highlights a large conformational change of the substrate binding domain that reflects the dynamic of the structure during the catalysis. In absence of the substrate, the domain is rotated and closes the substrate binding pocket. Upon incubation with Mg535 and a system for NADPH regeneration, the Mg534 product is converted to a compound with a retention time similar to UDP-GlcNAc
evolution
CapE belongs to a distinctive subfamily of SDR enzymes of pathogenic bacteria characterized by a singular catalytic triad displaying a Met residue (instead of the canonical Tyr residue) and a dynamic element known as the latch. Although CapE and FlaA1 afford the same product, the configuration of their active sites is different. Also, the latch region is absent in FlaA1
evolution
UDP-GlcNAc inverting 4,6-dehydratases can be divided into two subfamilies, based on the conservation of the canonical YXXXK motif at the active site, like FlaA1, or the presence of an altered motif, MXXXK, where the catalytic tyrosine is replaced by a methionine, represented by CapE. Mg534 is a 4,6-dehydratase 5-epimerase, its three-dimensional structure suggests that it belongs to a third subfamily of inverting dehydratases. The Mg534 protein exhibits the canonical catalytic triad containing the 140YXXXK144 motif present in other SDR enzymes
metabolism
conversion of UDP-D-GlcNAc into UDP-L-FucNAc, an essential precursor of capsular polysaccharide requires three enzymes CapE, CapF, and CapG in Staphylococcus aureus. CapE yields the first intermediate of the sequential reactions catalyzed by these three enzymes
metabolism
the first reaction that leads to the formation of the UDP-2-acetamido-2,6-dideoxy-beta-L-hexoses is the dehydration of UDP-D-GlcNAc catalyzed by enzyme Mg534. Mg534 is a 4,6-dehydratase 5-epimerase, an inverting dehydratase. Enzyme Mg535, next in the glycan synthesis pathway, is a bifunctional 3-epimerase 4-reductase. The sequential activity of the two enzymes leads to the formation of UDP-L-N-acetylrhamnosamine (UDP-L-RhaNAc). Pathway for the biosynthesis of UDP-2-acetamido-2,6-dideoxy-hexoses, overview
physiological function
CapE is an essential enzyme for the synthesis of capsular polysaccharide of pathogenic strains of Staphylococcus aureus
physiological function
the enzyme is involved in the Pse pathway for biosynthesis of glycans of the heavily glycosylated fibrils surrounding the viral capsids. Megavirus glycans are mainly composed of virally synthesized N-acetylglucosamine (GlcNAc). They also contain N-acetylrhamnosamine (RhaNAc), a rare sugar. The enzymes involved in its synthesis are encoded by a gene cluster specific to Megavirus close relatives. GC-MS analyses of Megavirus glycoconjugates
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D126N
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site-directed mutagenesis, the mutant shows about 100fold lower activity with UDP-GlcNAc and with UDP-6-deoxy-6-fluoro-GlcNAc for HF elimination compared to the wild-type enzyme. Upon addition of UDP-4-keto-6-deoxy-GlcNAc to D126N the tightly bound NADPH is immediately oxidized
K127A
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site-directed mutagenesis, the mutant shows about 100fold lower activity with UDP-GlcNAc and with UDP-6-deoxy-6-fluoro-GlcNAc for HF elimination compared to the wild-type enzyme. Upon addition of UDP-4-keto-6-deoxy-GlcNAc to K127A the tightly bound NADPH is immediately oxidized
Y135F
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site-directed mutagenesis, the mutant shows about 100fold lower activity with UDP-GlcNAc and with UDP-6-deoxy-6-fluoro-GlcNAc for HF elimination compared to the wild-type enzyme, slow oxidation of NADPH upon addition of UDP-4-keto-6-deoxy-GlcNAc to Y135F
C103M
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site-directed mutagenesis, the mutant is inactive, dimerization is prevented but the secondary structure is not significantly affected
C118M
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site-directed mutagenesis, not recombinantly expressable mutant
D149K/K150A
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site-directed mutagenesis, the mutant is inactive
D149K/K150D
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site-directed mutagenesis, the mutant is inactive
D70A
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site-directed mutagenesis, the mutant is inactive
D70N
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site-directed mutagenesis, not recombinantly expressable mutant
G20A
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site-directed mutagenesis, the mutant is inactive
H86A
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site-directed mutagenesis, insoluble protein, the mutant shows reduced activity compared to the wild-type enzyme
H86F
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site-directed mutagenesis, insoluble protein, the mutant is inactive
K133E
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site-directed mutagenesis, inactive mutant
K133M
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site-directed mutagenesis, inactive mutant
V266E
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y141F
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site-directed mutagenesis, the mutant is inactive
Y141M
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site-directed mutagenesis of a FlaA1 catalytic triad mutant, the mutant shows slightly reduced activity compared to the wild-type enzyme
F78W
site-directed mutagenesis of a cofactor binding residue, the mutant shows similar activity compared to the wild-type enzyme
L122F
site-directed mutagenesis of a cofactor binding residue, the mutant shows reduced activity compared to the wild-type enzyme
Y164A
site-directed mutagenesis of a cofactor binding residue, the mutant shows highly reduced activity compared to the wild-type enzyme
Y164F
site-directed mutagenesis of a cofactor binding residue, the mutant shows markedly reduced activity compared to the wild-type enzyme
additional information
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disruption of flaA1 and flaB1 genes by replacement of internal fragments with chloramphenicol and/or kanamycin gene cassettes. Both mutations selectively abolish expression of the targeted gene without affecting synthesis of the other flagellar polypeptide. flaA1 and flaB1 mutant strains exhibit altered motility in vitro and are less efficient in movement through a liquid medium. Paradoxically, isogenic strains containing specifically disrupted flaA1 or flaB1 alleles are capable of assembling periplasmic flagella that are morphologically wild-type, phenotype, detailed overview
additional information
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disruption of flaA1 and flaB1 genes by replacement of internal fragments with chloramphenicol and/or kanamycin gene cassettes. Both mutations selectively abolish expression of the targeted gene without affecting synthesis of the other flagellar polypeptide. flaA1 and flaB1 mutant strains exhibit altered motility in vitro and are less efficient in movement through a liquid medium. Paradoxically, isogenic strains containing specifically disrupted flaA1 or flaB1 alleles are capable of assembling periplasmic flagella that are morphologically wild-type, phenotype, detailed overview
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additional information
construction of flaA1 knockout mutant by gene disruption in strain NCTC 11637, the nonmotile mutant exhibits altered lipopolysaccharides, with loss of most O-antigen and core modification, and increased sensitivity to sodium dodecyl sulfate compared to wild-type bacteria. The flaA1 mutant produces flagellins but no flagellum. Phynotype, detailed overview
additional information
construction of flaA1 knockout mutant by gene disruption in strain NCTC 11637, the nonmotile mutant exhibits altered lipopolysaccharides, with loss of most O-antigen and core modification, and increased sensitivity to sodium dodecyl sulfate compared to wild-type bacteria. The flaA1 mutant produces flagellins but no flagellum. Phynotype, detailed overview
additional information
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construction of flaA1 knockout mutant by gene disruption in strain NCTC 11637, the nonmotile mutant exhibits altered lipopolysaccharides, with loss of most O-antigen and core modification, and increased sensitivity to sodium dodecyl sulfate compared to wild-type bacteria. The flaA1 mutant produces flagellins but no flagellum. Phynotype, detailed overview
additional information
-
construction of flaA1 knockout mutant by gene disruption in strain NCTC 11637, the nonmotile mutant exhibits altered lipopolysaccharides, with loss of most O-antigen and core modification, and increased sensitivity to sodium dodecyl sulfate compared to wild-type bacteria. The flaA1 mutant produces flagellins but no flagellum. Phynotype, detailed overview
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additional information
construction of a soluble truncated form of WbpM, His-S262
additional information
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construction of a soluble truncated form of WbpM, His-S262
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Morrison, J.P.; Schoenhofen, I.C.; Tanner, M.E.
Mechanistic studies on PseB of pseudaminic acid biosynthesis: a UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase
Bioorg. Chem.
36
312-320
2008
Campylobacter jejuni
brenda
McNally, D.J.; Schoenhofen, I.C.; Houliston, R.S.; Khieu, N.H.; Whitfield, D.M.; Logan, S.M.; Jarrell, H.C.; Brisson, J.
CMP-pseudaminic acid is a natural potent inhibitor of PseB, the first enzyme of the pseudaminic acid pathway in Campylobacter jejuni and Helicobacter pylori
ChemMedChem
3
55-59
2008
Helicobacter pylori
brenda
Schoenhofen, I.C.; McNally, D.J.; Brisson, J.; Logan, S.M.
Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction
Glycobiology
16
8C-14C
2006
Helicobacter pylori
brenda
Rosey, E.L.; Kennedy, M.J.; Petrella, D.K.; Ulrich, R.G.; Yancey, R.J.
Inactivation of Serpulina hyodysenteriae flaA1 and flaB1 periplasmic flagellar genes by electroporation-mediated allelic exchange
J. Bacteriol.
177
5959-5970
1995
Brachyspira hyodysenteriae, Brachyspira hyodysenteriae B204
brenda
Merkx-Jacques, A.; Obhi, R.K.; Bethune, G.; Creuzenet, C.
The Helicobacter pylori flaA1 and wbpB genes control lipopolysaccharide and flagellum synthesis and function
J. Bacteriol.
186
2253-2265
2004
Helicobacter pylori (Q6VYQ5), Helicobacter pylori (Q6VYQ6), Helicobacter pylori, Helicobacter pylori SS1 (Q6VYQ5), Helicobacter pylori NCTC 11637 (Q6VYQ6)
brenda
Creuzenet, C.; Schur, M.J.; Li, J.; Wakarchuk, W.W.; Lam, J.S.
FlaA1, a new bifunctional UDP-GlcNAc C6 Dehydratase/C4 reductase from Helicobacter pylori
J. Biol. Chem.
275
34873-34880
2000
Helicobacter pylori
brenda
Creuzenet, C.; Urbanic, R.V.; Lam, J.S.
Structure-function studies of two novel UDP-GlcNAc C6 dehydratases/C4 reductases. Variation from the SYK dogma
J. Biol. Chem.
277
26769-26778
2002
Helicobacter pylori
brenda
Ishiyama, N.; Creuzenet, C.; Miller, W.L.; Demendi, M.; Anderson, E.M.; Harauz, G.; Lam, J.S.; Berghuis, A.M.
Structural studies of FlaA1 from Helicobacter pylori reveal the mechanism for inverting 4,6-dehydratase activity
J. Biol. Chem.
281
24489-24495
2006
Helicobacter pylori
brenda
Schoenhofen, I.C.; McNally, D.J.; Vinogradov, E.; Whitfield, D.; Young, N.M.; Dick, S.; Wakarchuk, W.W.; Brisson, J.R.; 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
723-732
2006
Campylobacter jejuni, Helicobacter pylori, Campylobacter jejuni 11168
brenda
Creuzenet, C.; Lam, J.S.
Topological and functional characterization of WbpM, an inner membrane UDP-GlcNAc C6 dehydratase essential for lipopolysaccharide biosynthesis in Pseudomonas aeruginosa
Mol. Microbiol.
41
1295-1310
2001
Pseudomonas aeruginosa (P72145), Pseudomonas aeruginosa
brenda
Miyafusa, T.; Caaveiro, J.; Tanaka, Y.; Tsumoto, K.
Dynamic elements govern the catalytic activity of CapE, a capsular polysaccharide-synthesizing enzyme from Staphylococcus aureus
FEBS Lett.
587
3824-3830
2013
Staphylococcus aureus (A0A0H3JPH0)
brenda
Piacente, F.; De Castro, C.; Jeudy, S.; Molinaro, A.; Salis, A.; Damonte, G.; Bernardi, C.; Abergel, C.; Tonetti, M.G.
Giant virus Megavirus chilensis encodes the biosynthetic pathway for uncommon acetamido sugars
J. Biol. Chem.
289
24428-24439
2014
Megavirus chiliensis (G5CSR9)
brenda