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Literature summary extracted from

  • Joseph, D.D.; Jiao, W.; Parker, E.J.
    Arg314 is essential for catalysis by N-acetyl neuraminic acid synthase from Neisseria meningitidis (2013), Biochemistry, 52, 2609-2619.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

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
-
?

Organism

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
-

Substrates and Products (Substrate)

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
-
?

Subunits

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

Synonyms

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

General Information

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