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Information on EC 4.2.1.115 - UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting)
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4.2.1.115 UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting)IUBMB Comments
Contains NADP+ as a cofactor. This is the first enzyme in the biosynthetic pathway of pseudaminic acid , a sialic-acid-like sugar that is unique to bacteria and is used by Helicobacter pylori to modify its flagellin. This enzyme plays a critical role in H. pylori's pathogenesis, being involved in the synthesis of both functional flagella and lipopolysaccharides [1,2]. It is completely inhibited by UDP-alpha-D-galactose. The reaction results in the chirality of the C-5 atom being inverted. It is thought that Lys-133 acts sequentially as a catalytic acid, protonating the C-6 hydroxy group and as a catalytic base, abstracting the C-5 proton, resulting in the elimination of water. This enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes.
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Word Map
- 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
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
flaa1, cj1293, hp0840, mg534, udp-n-acetylglucosamine 5-inverting 4,6-dehydratase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cj1293
FlaA1
PseB
UDP-alpha-D-GlcNAc modifying dehydratase
UDP-GlcNAc C6 dehydratase
additional information
FlaA1
-
-
-
-
additional information
-
the enzyme is a member of the short chain dehydrogenase/reductase, SDR, family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
-
-
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UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
reaction mechanism
UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
Asp126, Lys127, and Tyr135 are the active site residues
-
UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
reaction mechanism of WbpM
UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
reaction mechanism, FlaA1 is a UDP-GlcNAc 4,6-dehydratase that additionally inverts the chirality at the C-5 position
-
UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
catalytic mechanism of CapE, overview. Tyr164 does not act as the general base as it does in SDR enzymes displaying the SYK triad motif
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetylglucosamine hydro-lyase (inverting; UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose-forming)
Contains NADP+ as a cofactor. This is the first enzyme in the biosynthetic pathway of pseudaminic acid [3], a sialic-acid-like sugar that is unique to bacteria and is used by Helicobacter pylori to modify its flagellin. This enzyme plays a critical role in H. pylori's pathogenesis, being involved in the synthesis of both functional flagella and lipopolysaccharides [1,2]. It is completely inhibited by UDP-alpha-D-galactose. The reaction results in the chirality of the C-5 atom being inverted. It is thought that Lys-133 acts sequentially as a catalytic acid, protonating the C-6 hydroxy group and as a catalytic base, abstracting the C-5 proton, resulting in the elimination of water. This enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes.
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CAS REGISTRY NUMBER
COMMENTARY
9076-60-2
-
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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
-
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
-
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
-
-
?
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
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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
-
-
?
UDP-N-acetylglucosamine
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + H2O
WbpM is specific for UDP-GlcNAc
-
-
?
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
-
-
?
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
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PseB catalyzes an additional C5 epimerization forming UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hexos-4-ulose
-
-
?
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
?
-
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
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
-
-
?
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
-
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 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
-
-
?
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-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
?
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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 LPS and flagellum production with glycosylation regulating the activity of these proteins
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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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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
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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 LPS and flagellum production with glycosylation regulating the activity of these proteins
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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
binding and binding site structure, overview. Function of Tyr164 is related to its bulkiness in the relay mechanism
NADPH
binding and binding site structure, overview. Function of Tyr164 is related to its bulkiness in the relay mechanism
NADPH
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
additional information
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the dehydratase does not require the addition of exogenous cofactor NAD(P)+
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additional information
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the dehydratase does not require the addition of exogenous cofactor NAD(P)+
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additional information
the hexose ring occupies a non-catalytic conformation with respect to the coenzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CMP-pseudaminic acid
-
mapping of the dynamic interactions of the enzyme with the inhibitor, overview
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dysentery
Dual flaA1 flaB1 mutant of Serpulina hyodysenteriae expressing periplasmic flagella is severely attenuated in a murine model of swine dysentery.
Infections
FlaA proteins in Leptospira interrogans are essential for motility and virulence but are not required for formation of the flagellum sheath.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.77
UDP-N-acetylglucosamine
pH 10.0, 30°C, recombinant soluble truncated WbpM mutant His-S262
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.8
UDP-N-acetylglucosamine
pH 10.0, 30°C, recombinant soluble truncated WbpM mutant His-S262
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000037
-
wild-type enzyme activity with UDP-6-deoxy-6-fluoro-GlcNAc for elimination of fluoride
0.23
-
wild-type enzyme activity with UDP-GlcNAc conversion to UDP-4-keto-6-deoxy-L-IdoNAc
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
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
Show AA Sequence and Transmembrane Helices (2014 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
x * 63000, recombinant N-terminally His-tagged WbpM, SDS-PAGE, x * 64000, recombinant C-terminally His-tagged WbpM, SDS-PAGE, x * 60000, recombinant His-tagged truncated WbpM, SDS-PAGE
63000
x * 63000, recombinant N-terminally His-tagged WbpM, SDS-PAGE, x * 64000, recombinant C-terminally His-tagged WbpM, SDS-PAGE, x * 60000, recombinant His-tagged truncated WbpM, SDS-PAGE
64000
x * 63000, recombinant N-terminally His-tagged WbpM, SDS-PAGE, x * 64000, recombinant C-terminally His-tagged WbpM, SDS-PAGE, x * 60000, recombinant His-tagged truncated WbpM, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 63000, recombinant N-terminally His-tagged WbpM, SDS-PAGE, x * 64000, recombinant C-terminally His-tagged WbpM, SDS-PAGE, x * 60000, recombinant His-tagged truncated WbpM, SDS-PAGE
hexamer