EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.56 | phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O | Neisseria meningitidis | - |
phosphate + N-acetylneuraminate | - |
? | |
2.5.1.56 | phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O | Neisseria meningitidis MC58 | - |
phosphate + N-acetylneuraminate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.56 | Neisseria meningitidis | H2VFG5 | serotype B, gene synC | - |
2.5.1.56 | Neisseria meningitidis MC58 | H2VFG5 | serotype B, gene synC | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.56 | phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O | - |
Neisseria meningitidis | phosphate + N-acetylneuraminate | - |
? | |
2.5.1.56 | phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O | - |
Neisseria meningitidis MC58 | phosphate + N-acetylneuraminate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.5.1.56 | More | the enzyme contains an antifreeze protein like (AFPL) domain, which extends from the C-terminal of the (beta/alpha)8 barrel containing the active site and contributes a highly conserved arginine, Arg314, into the active site of the opposing monomer chain | Neisseria meningitidis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.56 | NANA synthase | - |
Neisseria meningitidis |
2.5.1.56 | NANAS | - |
Neisseria meningitidis |
2.5.1.56 | NeuB | - |
Neisseria meningitidis |
2.5.1.56 | NmeNANAS | - |
Neisseria meningitidis |
2.5.1.56 | sialic acid synthase | - |
Neisseria meningitidis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.5.1.56 | additional information | residue Arg314 is essential for catalysis, the delocalized positively charged guanidinium functionality of this residue provides steering of the sugar substrate ManNAc for suitable placement in the active site and thus reaction with phosphoenolpyruvate | Neisseria meningitidis |
2.5.1.56 | physiological function | sialic acid N-acetylneuraminic acid (NANA) has a key role in the pathogenesis of a select number of neuroinvasive bacteria such as Neisseria meningitidis. These pathogens coat themselves with polysialic acids, mimicking the exterior surface of mammalian cells and consequentially concealing the bacteria from the host's immune system. N-acetylneuraminic acid is synthesized in bacteria by the homodimeric enzyme NANA synthase (NANAS), which catalyzes a condensation reaction between phosphoenolpyruvate (PEP) and N-acetylmannosamine | Neisseria meningitidis |