General Stability | Organism |
---|---|
the purified enzyme is 80% pure, no further purification because it is unstable to freezing and has limited stability upon storage at 4°C | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.026 | - |
UDP-N-acetyl-D-glucosamine | 37°C, pH 7.5 | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Rattus norvegicus | the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/ManNAc kinase catalyzes the first two steps in the biosynthesis of the sialic acids | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme expressed in Spodoptera frugiperda cells using a baculovirus expression system | Rattus norvegicus |
Storage Stability | Organism |
---|---|
4°C, purified enzyme is 80% pure, no further purification because it is unstable to freezing and has limited stability upon storage at 4°C | Rattus norvegicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | reaction mechanism involving an anti-elimination of UDP to give 2-acetamidoglucal, followed by a syn-addition of water | Rattus norvegicus | ? | - |
? | |
additional information | the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/ManNAc kinase catalyzes the first two steps in the biosynthesis of the sialic acids | Rattus norvegicus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
More | bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/ManNAc kinase | Rattus norvegicus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.33 | - |
UDP-N-acetyl-D-glucosamine | 37°C, pH 7.5 | Rattus norvegicus |