4.2.1.115: UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting)
This is an abbreviated version!
For detailed information about UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting), go to the full flat file.
Word Map on EC 4.2.1.115
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4.2.1.115
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flagellins
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spirochete
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pylori
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flagella
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helicobacter
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jejuni
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campylobacter
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hyodysenteriae
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pseudaminic
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serpulina
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flab
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sheath
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interrogans
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hexameric
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dysentery
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o-antigen
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non-motile
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leptospiral
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enteropathogenicity
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pilosicoli
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innocens
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udp-n-acetyl-d-glucosamine
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brachyspira
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ecorv
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bacillosamine
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syk
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drug development
- 4.2.1.115
- flagellins
-
spirochete
- pylori
-
flagella
- helicobacter
- jejuni
- campylobacter
- hyodysenteriae
-
pseudaminic
- serpulina
-
flab
-
sheath
- interrogans
-
hexameric
- dysentery
-
o-antigen
-
non-motile
-
leptospiral
-
enteropathogenicity
- pilosicoli
- innocens
- udp-n-acetyl-d-glucosamine
- brachyspira
- ecorv
-
bacillosamine
- syk
- drug development
Reaction
Synonyms
4,6-dehydratase/5-epimerase, CapE, Cj1293, FlaA1, HP0840, inverting 4,6-dehydratase, Mg534, More, NAD(P)+-dependent dehydratase/epimerase, PseB, UDP-alpha-D-GlcNAc modifying dehydratase, UDP-GlcNAc 5-inverting 4,6-dehydratase, UDP-GlcNAc C6 dehydratase, UDP-GlcNAc C6 dehydratase/C4 reductase, UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase, WbpM
ECTree
4.2.1.115 UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting)Advanced search results
results (
results (Substrates Products
Substrates Products on EC 4.2.1.115 - UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting)
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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
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
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elimination of fluoride from the substrate by the wild-type PseB, no activity by mutant enzymes K127A, D126N, and Y135F
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
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
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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
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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
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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
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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
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the enzyme is involved in the pseudaminic acid biosynthesis, it is responsible for the biosynthesis of 6-deoxyhexose
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-
?
UDP-GlcNAc
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hexos-4-ulose + H2O
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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
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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
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
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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
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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
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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
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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
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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
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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
-
-
?
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
-
-
?
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
?
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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
?
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-
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
-
-
?
additional information
?
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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
?
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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
?
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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
?
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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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-
?
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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?
