EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    2.5.1.56 | 2-acetamido-6-azido-2,6-dideoxy-D-mannose + phosphoenolpyruvate + H2O |
- |
Neisseria meningitidis |
5-acetamido-9-azido-3,5,9-trideoxy-D-glycero-D-galacto-2-nonulosonic acid + phosphate |
- |
? |
| 2.5.1.56 | 2-acetamido-6-azido-2,6-dideoxy-D-mannose + phosphoenolpyruvate + H2O |
- |
Neisseria meningitidis 60E |
5-acetamido-9-azido-3,5,9-trideoxy-D-glycero-D-galacto-2-nonulosonic acid + phosphate |
- |
? |
| 2.5.1.56 | more |
arginine residues are present in the active site and are involved in substrate recognition and binding |
Streptococcus agalactiae |
? |
- |
? |
| 2.5.1.56 | more |
enzyme catalyzes the condensation of the si face of phosphoenolpyruvate with the aldehyde sugar |
Campylobacter jejuni |
? |
- |
? |
| 2.5.1.56 | more |
binding of phosphoenolpyruvate is associated with a change in the average conformation of enzyme NmeNANAS causing changes in flexibility in both AFPL domain and ManNAc binding loop |
Neisseria meningitidis |
? |
- |
? |
| 2.5.1.56 | more |
the enzyme shows activity towards 2-acetamido-4-O-acetyl-2-deoxy-D-mannopyranose resulting in formation of 4-O-acetyl-ManNAc |
Idiomarina loihiensis |
? |
- |
? |
| 2.5.1.56 | more |
the enzyme shows activity towards 2-acetamido-4-O-acetyl-2-deoxy-D-mannopyranose resulting in formation of 4-O-acetyl-ManNAc |
Idiomarina loihiensis L2-TR |
? |
- |
? |
| 2.5.1.56 | more |
binding of phosphoenolpyruvate is associated with a change in the average conformation of enzyme NmeNANAS causing changes in flexibility in both AFPL domain and ManNAc binding loop |
Neisseria meningitidis MC58 |
? |
- |
? |
| 2.5.1.56 | N-acetyl-D-galactosamine + phosphoenolpyruvate + H2O |
15% of the activity with N-acetyl-D-mannosamine |
Streptococcus agalactiae |
? |
- |
? |
| 2.5.1.56 | N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O |
- |
Escherichia coli |
N-acetylneuraminate + phosphate |
- |
? |
