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show all sequences of 2.6.1.98

Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1

Larkin, A.; Imperiali, B.; Biochemistry 48, 5446-5455 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene wpbE, overexpression of N-terminally T7- and C-terminally His6-tagged WpbE in Escherichia coli strain BL21-CodonPlus(DE3)RIL
Pseudomonas aeruginosa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
Pseudomonas aeruginosa
-
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas aeruginosa
-
gene wbpE
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged WpbE from Escherichia coli strain BL21-CodonPlus(DE3)RIL by nickel affinity chromatography
Pseudomonas aeruginosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
WbpB and WbpE are a dehydrogenase/aminotransferase pair that converts UDP-N-acetyl-D-glucosaminuronate, UDP-GlcNAcA, to UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronate, UDP-GlcNAc(3NH2)A, in a coupled reaction via a unique NAD+ recycling pathway, large-scale coupled reaction WpbB/WpbE, overview. WbpA, WbpB, WbpE, WbpD and WbpI can be combined in vitro to generate UDP-ManNAc(3NAc)A in a single reaction vessel. Addition of 0.2 mM NAD+, for WbpB, and 0.1 mM pyridoxal 5'-phosphate, for WbpE, to the reaction mixture aids in achieving complete turnover of substrate, which implies that the heterologously expressed proteins are not saturated with cofactor due to the limiting intracellular levels of both NAD+ and pyridoxal 5'-phosphate in Escherichia coli. WbpB/WbpE substrate specificity, overview
718852
Pseudomonas aeruginosa
?
-
-
-
-
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
-
718852
Pseudomonas aeruginosa
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
r
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Pseudomonas aeruginosa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8
assay at
Pseudomonas aeruginosa
Cofactor
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
-
Pseudomonas aeruginosa
Cloned(Commentary) (protein specific)
Commentary
Organism
gene wpbE, overexpression of N-terminally T7- and C-terminally His6-tagged WpbE in Escherichia coli strain BL21-CodonPlus(DE3)RIL
Pseudomonas aeruginosa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
-
Pseudomonas aeruginosa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
Pseudomonas aeruginosa
-
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged WpbE from Escherichia coli strain BL21-CodonPlus(DE3)RIL by nickel affinity chromatography
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
WbpB and WbpE are a dehydrogenase/aminotransferase pair that converts UDP-N-acetyl-D-glucosaminuronate, UDP-GlcNAcA, to UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronate, UDP-GlcNAc(3NH2)A, in a coupled reaction via a unique NAD+ recycling pathway, large-scale coupled reaction WpbB/WpbE, overview. WbpA, WbpB, WbpE, WbpD and WbpI can be combined in vitro to generate UDP-ManNAc(3NAc)A in a single reaction vessel. Addition of 0.2 mM NAD+, for WbpB, and 0.1 mM pyridoxal 5'-phosphate, for WbpE, to the reaction mixture aids in achieving complete turnover of substrate, which implies that the heterologously expressed proteins are not saturated with cofactor due to the limiting intracellular levels of both NAD+ and pyridoxal 5'-phosphate in Escherichia coli. WbpB/WbpE substrate specificity, overview
718852
Pseudomonas aeruginosa
?
-
-
-
-
UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate + 2-oxoglutarate
-
718852
Pseudomonas aeruginosa
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + L-glutamate
-
-
-
r
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Pseudomonas aeruginosa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8
assay at
Pseudomonas aeruginosa
General Information
General Information
Commentary
Organism
metabolism
the biosynthetic pathway begins with WbpA, catalyzing the C6-oxidation of UDP-GlcNAc to give the corresponding UDP-N-acetyl-D-glucosaminuronic acid. The C3-dehydrogenase WbpB, aminotransferase WbpE, and acetyltransferase WbpD sequentially convert UDP-GlcNAcA into UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronic acid. Finally, the C2-epimerase WbpI modifies UDP-GlcNAc(3NAc)A to give the final UDP-ManNAc(3NAc)A
Pseudomonas aeruginosa
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the biosynthetic pathway begins with WbpA, catalyzing the C6-oxidation of UDP-GlcNAc to give the corresponding UDP-N-acetyl-D-glucosaminuronic acid. The C3-dehydrogenase WbpB, aminotransferase WbpE, and acetyltransferase WbpD sequentially convert UDP-GlcNAcA into UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronic acid. Finally, the C2-epimerase WbpI modifies UDP-GlcNAc(3NAc)A to give the final UDP-ManNAc(3NAc)A
Pseudomonas aeruginosa
Other publictions for EC 2.6.1.98
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
737244
Shoji
Involvement of the Wbp pathway ...
Porphyromonas gingivalis, Porphyromonas gingivalis DSM 20709
Sci. Rep.
4
5056
2014
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1
1
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707534
Larkin
Structural analysis of WbpE fr ...
Pseudomonas aeruginosa
Biochemistry
49
7227-7237
2010
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1
1
9
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1
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3
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1
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1
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9
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1
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1
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2
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4
4
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709007
Westman
Characterization of WbpB, WbpE ...
Pseudomonas aeruginosa
J. Biol. Chem.
284
11854-11862
2009
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1
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1
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1
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1
1
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1
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1
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2
3
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1
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1
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1
1
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718852
Larkin
Biosynthesis of UDP-GlcNAc(3NA ...
Pseudomonas aeruginosa
Biochemistry
48
5446-5455
2009
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1
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1
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1
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1
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2
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1
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1
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1
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1
1
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1
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1
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1
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1
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1
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692874
Westman
Biosynthesis of a rare di-N-ac ...
Bordetella pertussis, Pseudomonas aeruginosa
J. Bacteriol.
190
6060-6069
2008
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2
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1
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2
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2
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2
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2
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2
2
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1
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2
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2
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4
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