EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.1.60 | overexpression of active enzyme by using the baculovirus/Sf9 system | Rattus norvegicus |
5.1.3.14 | high level overexpression of the active enzyme is established by using the baculovirus/Sf9 system | Rattus norvegicus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.1.60 | D413K | loss of kinase activity | Rattus norvegicus |
2.7.1.60 | D413L | loss of kinase activity | Rattus norvegicus |
2.7.1.60 | D413N | loss of kinase activity | Rattus norvegicus |
2.7.1.60 | H110A | loss of epimerase activity | Rattus norvegicus |
2.7.1.60 | H132A | loss of epimerase activity | Rattus norvegicus |
2.7.1.60 | H155A | loss of epimerase activity | Rattus norvegicus |
2.7.1.60 | H157A | loss of epimerase activity | Rattus norvegicus |
2.7.1.60 | H45A | loss of epimerase activity | Rattus norvegicus |
2.7.1.60 | R420M | loss of kinase activity | Rattus norvegicus |
5.1.3.14 | D413K | enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity | Rattus norvegicus |
5.1.3.14 | D413N | enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity | Rattus norvegicus |
5.1.3.14 | H110A | mutant enzyme shows a drastic loss of epimerase activity, oligomerization is significantly different from that of the wild-type enzyme,loss of epimerase activity can largely by attributed to incorrect protein folding | Rattus norvegicus |
5.1.3.14 | H132A | mutant enzyme shows a drastic loss of epimerase activity, oligomerization is significantly different from that of the wild-type enzyme, loss of epimerase activity can largely by attributed to incorrect protein folding | Rattus norvegicus |
5.1.3.14 | H155A | mutant enzyme forms mainly trimeric enzyme with small amounts of hexamer | Rattus norvegicus |
5.1.3.14 | H155A | mutant enzyme shows a drastic loss of epimerase activity, loss of epimerase activity can largely by attributed to incorrect protein folding | Rattus norvegicus |
5.1.3.14 | H157A | mutant enzyme forms mainly trimeric enzyme with small amounts of hexamer | Rattus norvegicus |
5.1.3.14 | H157A | mutant enzyme shows a drastic loss of epimerase activity, loss of epimerase activity can largely by attributed to incorrect protein folding | Rattus norvegicus |
5.1.3.14 | H45A | mutant enzyme shows a drastic loss of epimerase activity | Rattus norvegicus |
5.1.3.14 | R420M | enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity | Rattus norvegicus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
5.1.3.14 | CMP-N-acetylneuraminic acid | feedback inhibitor | Rattus norvegicus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.7.1.60 | cytosol | - |
Rattus norvegicus | 5829 | - |
5.1.3.14 | cytosol | - |
Rattus norvegicus | 5829 | - |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.7.1.60 | 75000 | - |
gel filtration, SDS-PAGE | Rattus norvegicus |
2.7.1.60 | 450000 | - |
gel filtration | Rattus norvegicus |
5.1.3.14 | 75000 | - |
6 * 75000, SDS-PAGE | Rattus norvegicus |
5.1.3.14 | 450000 | - |
gel filtration | Rattus norvegicus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.60 | ATP + N-acetyl-D-mannosamine | Rattus norvegicus | involved in N-acetylneuraminic acid metabolism, key enzyme in N-acetylneuraminic acid biosynthesis | ADP + N-acetyl-D-mannosamine 6-phosphate | - |
? | |
5.1.3.14 | additional information | Rattus norvegicus | key enzyme of N-acetylneuraminic acid biosynthesis | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.1.60 | Rattus norvegicus | - |
- |
- |
5.1.3.14 | Rattus norvegicus | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.7.1.60 | liver | - |
Rattus norvegicus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.7.1.60 | 0.84 | - |
recombinant enzyme | Rattus norvegicus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.60 | ATP + N-acetyl-D-mannosamine | involved in N-acetylneuraminic acid metabolism, key enzyme in N-acetylneuraminic acid biosynthesis | Rattus norvegicus | ADP + N-acetyl-D-mannosamine 6-phosphate | - |
? | |
2.7.1.60 | ATP + N-acetyl-D-mannosamine | - |
Rattus norvegicus | ADP + N-acetyl-D-mannosamine-6-phosphate | - |
? | |
5.1.3.14 | additional information | bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase | Rattus norvegicus | ? | - |
? | |
5.1.3.14 | additional information | key enzyme of N-acetylneuraminic acid biosynthesis | Rattus norvegicus | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.1.60 | dimer | 2 * 75000, self associates as a dimer, gel filtration, SDS-PAGE, catalyzes only phosphorylation of N-acetylmannosamine, incubation with UDP-N-acetylglucosamine leads to reassembly of the fully active hexamer | Rattus norvegicus |
2.7.1.60 | hexamer | - |
Rattus norvegicus |
5.1.3.14 | hexamer | 6 * 75000, SDS-PAGE | Rattus norvegicus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.1.60 | EC 5.1.3.14/EC 2.7.1.60 | - |
Rattus norvegicus |
2.7.1.60 | UDP-GlcNAc-epimerase/ManNAc kinase | - |
Rattus norvegicus |
5.1.3.14 | More | bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase | Rattus norvegicus |