EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    5.1.3.14 | UDP-N-acetyl-D-glucosamine |
possible role in the biogenesis of N-acetylmannosamine-containing macromolecules |
Rattus norvegicus |
? |
- |
? |
| 5.1.3.14 | UDP-N-acetyl-D-glucosamine |
r |
Escherichia coli |
UDP-N-acetyl-D-mannosamine |
- |
? |
| 5.1.3.14 | more |
rate-limiting step in sialic acid biosynthesis pathway. The enzyme is the major determinant of cell surface sialylation in hematopoietic cell lines and is a critical regulator of the function of specific cell surface adhesion molecules |
Homo sapiens |
? |
- |
? |
| 5.1.3.14 | more |
reaction mechanism involving an anti-elimination of UDP to give 2-acetamidoglucal, followed by a syn-addition of water |
Rattus norvegicus |
? |
- |
? |
| 5.1.3.14 | UDP-N-acetyl-D-glucosamine |
reduction of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase activity and sialylation in distal myopathy with rimmed vacuoles |
Homo sapiens |
UDP-N-acetyl-D-mannosamine |
- |
? |
| 5.1.3.14 | UDP-N-acetyl-D-glucosamine |
reversibility is not detected |
Rattus norvegicus |
UDP-N-acetyl-D-mannosamine |
- |
? |
| 5.1.3.14 | more |
role of splice variant GNE1 in basic supply of cells with sialic acids, whereas GNE2 and GNE3 may have a function in finetuning of the sialic acid pathway |
Homo sapiens |
? |
- |
? |
| 5.1.3.14 | more |
role of splice variant GNE1 in basic supply of cells with sialic acids, whereas GNE2 and GNE3 may have a function in finetuning of the sialic acid pathway. No significant differences in activities of splice variants mGNE 1 and mGNE2 |
Mus musculus |
? |
- |
? |
| 5.1.3.14 | UDP-GlcNAc |
sialic acid biosynthetic pathway |
Homo sapiens |
ManNAc + UDP |
- |
? |
| 5.1.3.14 | more |
substrate specificity, overview. Recombinant His6-tagged NmSacA-His6 can tolerate several chemoenzymatically synthesized UDP-ManNAc derivatives as substrates in the absence of UDP-GlcNAc although its activity is much lower than with non-modified UDP-ManNAc. Homology modeling and molecular docking. The formation of UDP-GlcNAc or UDP-ManNAc is not observed by incubating NmSacA-His6 with 2-acetamidoglucal and UDP in contrast to the serogroup B enzyme. No enzyme activity with UDP-mannose, UDP-ManF, UDP-ManN3, UDP-ManNH2, uridine 5'-diphospho-2-butyramido-2-deoxy-alpha-D-mannopyranoside, uridine 5'-diphospho-2-azidoacetamido-2-deoxy-alpha-D-mannopyranoside, uridine 5'-diphospho-2-phenylacetamido-2-deoxy-alpha-D-mannopyranoside, dihydropyrimidine-2, 4(1H,3H)-dione-alpha-D-ribofuranosyl-5'-diphospho-2-azidoxyacetamido-2-deoxy-alpha-D-mannopyranoside, and uridine 5'-diphospho-2-azidoacetamido-2-deoxy-alpha-D-glucopyranoside, docking study |
Neisseria meningitidis serogroup A / serotype 4A |
? |
- |
? |
