EC Number | Application | Comment | Organism |
---|---|---|---|
2.4.3.1 | biotechnology | recombinant enzyme may be used for in vitro synthesis of oligosaccharides | Homo sapiens |
2.4.3.1 | synthesis | recombinant enzyme may be used for in vitro synthesis of oligosaccharides | Homo sapiens |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.4.3.1 | expression in Pichia pastoris, entry in the secretory pathway, i.e. excretion of the soluble enzyme to the medium, by usage of the N-terminal signal sequence of Saccharomyces cerevisiae alpha-factor, no hyperglycosylation | Homo sapiens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.4.3.1 | 0.15 | - |
CMP-N-acetylneuraminate | recombinant enzyme | Homo sapiens | |
2.4.3.1 | 2.3 | - |
N-acetyllactosamine | recombinant enzyme | Homo sapiens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.3.1 | Homo sapiens | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
2.4.3.1 | glycoprotein | 2times N-glycosylated | Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.3.1 | CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine | i.e. N-acetyllactosamine | Homo sapiens | CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine | - |
? | |
2.4.3.1 | CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R | sialic acid is linked to C-6 of the galactose residue | Homo sapiens | CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-R | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.3.1 | 37 | - |
assay at | Homo sapiens |