EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.367 | expression in Escherichia coli | Pseudomonas aeruginosa |
1.1.1.367 | expression in Escherichia coli | Staphylococcus aureus |
5.1.3.28 | expressed in Escherichia coli | Staphylococcus aureus |
5.1.3.28 | expressed in Escherichia coli | Pseudomonas aeruginosa |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.1.367 | 43600 | - |
x * 43600, SDS-PAGE | Pseudomonas aeruginosa |
1.1.1.367 | 43600 | - |
x * 43600, SDS-PAGE | Staphylococcus aureus |
5.1.3.28 | 43900 | - |
x * 43900, calculated from amino acid sequence | Staphylococcus aureus |
5.1.3.28 | 43900 | - |
x * 43900, calculated from amino acid sequence | Pseudomonas aeruginosa |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.367 | Pseudomonas aeruginosa | - |
- |
- |
1.1.1.367 | Pseudomonas aeruginosa O11 | - |
- |
- |
1.1.1.367 | Staphylococcus aureus | P95700 | - |
- |
1.1.1.367 | Staphylococcus aureus Newman | P95700 | - |
- |
5.1.3.28 | Pseudomonas aeruginosa | - |
- |
- |
5.1.3.28 | Pseudomonas aeruginosa O11 | - |
- |
- |
5.1.3.28 | Staphylococcus aureus | - |
- |
- |
5.1.3.28 | Staphylococcus aureus Newman | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
5.1.3.28 | nickel chelating column chromatography | Staphylococcus aureus |
5.1.3.28 | nickel chelating column chromatography | Pseudomonas aeruginosa |
EC Number | Storage Stability | Organism |
---|---|---|
1.1.1.367 | -20°C, 40% glycerol, stable for several weeks | Pseudomonas aeruginosa |
1.1.1.367 | -20°C, 40% glycerol, stable for several weeks | Staphylococcus aureus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.367 | UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+ | - |
Staphylococcus aureus | UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+ | enzyme Cap5F is responsible for the reduction at C4 of UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose | ? | |
1.1.1.367 | UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+ | - |
Pseudomonas aeruginosa | UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+ | enzyme WbjC is responsible for the reduction at C4 of UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose | ? | |
1.1.1.367 | UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+ | - |
Staphylococcus aureus Newman | UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+ | enzyme Cap5F is responsible for the reduction at C4 of UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose | ? | |
1.1.1.367 | UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+ | - |
Pseudomonas aeruginosa O11 | UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+ | enzyme WbjC is responsible for the reduction at C4 of UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose | ? | |
5.1.3.28 | additional information | no activity with UDP-D-GlcNAc | Staphylococcus aureus | ? | - |
? | |
5.1.3.28 | additional information | no activity with UDP-D-GlcNAc | Pseudomonas aeruginosa | ? | - |
? | |
5.1.3.28 | additional information | no activity with UDP-D-GlcNAc | Staphylococcus aureus Newman | ? | - |
? | |
5.1.3.28 | additional information | no activity with UDP-D-GlcNAc | Pseudomonas aeruginosa O11 | ? | - |
? | |
5.1.3.28 | UDP-2-acetamido-2,6-dideoxy-beta-L-talose | - |
Staphylococcus aureus | UDP-N-acetyl-beta-L-fucosamine | - |
? | |
5.1.3.28 | UDP-2-acetamido-2,6-dideoxy-beta-L-talose | - |
Pseudomonas aeruginosa | UDP-N-acetyl-beta-L-fucosamine | - |
? | |
5.1.3.28 | UDP-2-acetamido-2,6-dideoxy-beta-L-talose | - |
Staphylococcus aureus Newman | UDP-N-acetyl-beta-L-fucosamine | - |
? | |
5.1.3.28 | UDP-2-acetamido-2,6-dideoxy-beta-L-talose | - |
Pseudomonas aeruginosa O11 | UDP-N-acetyl-beta-L-fucosamine | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.367 | ? | x * 43600, SDS-PAGE | Pseudomonas aeruginosa |
1.1.1.367 | ? | x * 43600, SDS-PAGE | Staphylococcus aureus |
5.1.3.28 | ? | x * 43900, calculated from amino acid sequence | Staphylococcus aureus |
5.1.3.28 | ? | x * 43900, calculated from amino acid sequence | Pseudomonas aeruginosa |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.367 | Cap5F | - |
Staphylococcus aureus |
1.1.1.367 | O11 O-antigen biosynthesis associated epimerase | - |
Pseudomonas aeruginosa |
1.1.1.367 | WbjC | - |
Pseudomonas aeruginosa |
5.1.3.28 | Cap5G | - |
Staphylococcus aureus |
5.1.3.28 | WbjD | - |
Pseudomonas aeruginosa |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.367 | physiological function | involved in biosynthesis of N-acetyl-L-fucosamine. Enzyme Cap5E catalyzes 4,6-dehydration of UDP-N-acetyl-Dglucosamine and 3- and 5-epimerization to yield a mixture of three keto-deoxy-sugars. UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose is subsequently reduced at C4 to UDP-2-acetamido-2,6-dideoxy-L-talose by Cap5F. Incubation of UDP-2-acetamido-2,6-dideoxy-L-talose with Cap5G results in 2-epimerization to N-acetyl-L-fucosamine | Staphylococcus aureus |
1.1.1.367 | physiological function | involved in biosynthesis of N-acetyl-L-fucosamine. Enzyme WbjB catalyzes 4,6-dehydration of UDP-N-acetyl-Dglucosamine and 3- and 5-epimerization to yield a mixture of three keto-deoxy-sugars. UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose is subsequently reduced at C4 to UDP-2-acetamido-2,6-dideoxy-L-talose by WbjC. Incubation of UDP-2-acetamido-2,6-dideoxy-L-talose with WbjD results in 2-epimerization to N-acetyl-L-fucosamine | Pseudomonas aeruginosa |