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Literature summary for 1.1.1.335 extracted from
- 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 (2009), Biochemistry, 48, 5446-5455.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 2-oxoglutarate | required as oxidant for NAD+ recycling, product of 2-oxoglutarate reduction is 2-hydroxyglutarate | Pseudomonas aeruginosa |  |
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | enzyme WbpB and the related enzymes of the B-band O-antigen pathway of Pseudomonas aeruginosa lipopolysaccharide, WbpA, WbpE, WbpD and WbpI, can be combined in vitro to generate UDP-ManNAc(3NAc)A in a single reaction vessel, thereby providing supplies of this complex glycosyl donor for future studies of lipopolysaccharide assembly | Pseudomonas aeruginosa |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Pseudomonas aeruginosa |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 38271 | - |
x * 38271, calculated for recombinant enzyme including His- and T7 tags | Pseudomonas aeruginosa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | G3XD23 | - |
- |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -20°C, stable for at least 3 months | Pseudomonas aeruginosa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-2-acetamido-2-deoxy-alpha-D-glucuronate + NAD+ | isolated enzyme EWbpB in presence of UDP-2-acetamido-2-deoxy-alpha-D-glucuronate and NAD+ does not show enzymic activity. Upon the addition of WbpE and L-glutamate to the reaction, complete turnover of the starting material and the formation of UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid are observed. No turnover is observed in the presence of UDP-N-acetyl-D-glucosamine or UDP-UDP-N-acetyl-D-galactosamine, and only minimal turnover is observed when UDP-D-glucuronic acid is used as the nucleotide sugar substrate. Enzyme WbpB prefers the glucopyranose configuration of the sugar as well as the presence of both the carboxylate at the C'' carbon and the acetylated amine at the C'' position. WbpE is specific for L-glutamate as the amine donor. Presence of 2-ketoglutarate is required as oxidant for NAD+ recycling | Pseudomonas aeruginosa | UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH + H+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 38271, calculated for recombinant enzyme including His- and T7 tags | Pseudomonas aeruginosa |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| WbpB | - |
Pseudomonas aeruginosa |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
coupled reaction of enzymes WbpB/WbpE | Pseudomonas aeruginosa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
coupled reaction of enzymes WbpB/WbpE | Pseudomonas aeruginosa |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Pseudomonas aeruginosa | |
| NADH | - |
Pseudomonas aeruginosa | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | enzyme WbpB is part of the B-band O-antigen pathway of Pseudomonas aeruginosa lipopolysaccharide. Proteins WbpB and WbpE are a dehydrogenase/aminotransferase pair that converts UDP-GlcNAcA to UDP-GlcNAc(3NH2)A in a coupled reaction via a NAD+ recycling pathway | Pseudomonas aeruginosa |
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