BRENDA - Enzyme Database
show all sequences of 1.1.1.335

Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid

Thoden, J.; Holden, H.; Biochemistry 49, 7939-7948 (2010)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Escherichia coli
Pseudomonas aeruginosa
expression in Escherichia coli
Thermus thermophilus
Crystallization (Commentary)
Crystallization (Commentary)
Organism
crystal structure of the enzyme in a complex with NAD(H), to 1.5 A resolution. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft
Pseudomonas aeruginosa
crystal structures of the enzyme in a complex with NAD(H) and 2-oxoglutarate, and the enzyme in a complex with NAD(H) and its substrate UDP-N-acetyl-D-glucosaminuronic acid, to 1.45 A and 2.0 A resolution, respectively. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft. Residues Lys101 and His185 most likely play key roles in catalysis
Thermus thermophilus
Organism
Organism
UniProt
Commentary
Textmining
Pseudomonas aeruginosa
G3XD23
-
-
Thermus thermophilus
Q72KX8
-
-
Synonyms
Synonyms
Commentary
Organism
WblA
-
Pseudomonas aeruginosa
WblA
-
Thermus thermophilus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Pseudomonas aeruginosa
expression in Escherichia coli
Thermus thermophilus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure of the enzyme in a complex with NAD(H), to 1.5 A resolution. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft
Pseudomonas aeruginosa
crystal structures of the enzyme in a complex with NAD(H) and 2-oxoglutarate, and the enzyme in a complex with NAD(H) and its substrate UDP-N-acetyl-D-glucosaminuronic acid, to 1.45 A and 2.0 A resolution, respectively. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft. Residues Lys101 and His185 most likely play key roles in catalysis
Thermus thermophilus
Other publictions for EC 1.1.1.335
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
Synonyms
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)
743790
Shoji
Involvement of the Wbp pathwa ...
Porphyromonas gingivalis, Porphyromonas gingivalis DSM 20709
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1
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1
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2
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2
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2
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1
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1
1
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1
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2
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2
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Bordetella pertussis, Chromobacterium violaceum
Biochemistry
50
1483-1491
2011
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2
2
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8
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2
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6
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2
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6
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2
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2
2
2
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8
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6
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6
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6
6
718882
Thoden
Structural and functional stud ...
Pseudomonas aeruginosa, Thermus thermophilus
Biochemistry
49
7939-7948
2010
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2
2
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2
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709007
Westman
Characterization of WbpB, WbpE ...
Pseudomonas aeruginosa
J. Biol. Chem.
284
11854-11862
2009
-
1
1
-
-
-
-
-
-
-
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1
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1
1
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1
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
1
1
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
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1
1
1
2
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1
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1
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1
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1
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