EC Number   |
General Information |
Reference |
|---|
    2.5.1.56 | malfunction |
a truncated variant of the enzyme lacking the C-terminal AFPL domain is soluble and catalytically inactive, loss of the AFPL domain destabilizes the dimeric form of the enzyme. The AFPL domain plays a critical role for both the catalytic function and quaternary structure stability of N-acetylneuraminic acid synthase. phosphoenolpyruvate has a major effect on the thermal stability of the enzyme and loss of the AFPL domain in mutant G272Term eliminates this property |
-, 739614 |
| 2.5.1.56 | malfunction |
biallelic mutations in gene NANS, the gene encoding N-acetylneuraminic acid synthase, in nine individuals causes infantile-onset severe developmental delay and skeletal dysplasia. The main clinical features of the disorder included a prenatal history that is unremarkable in all patients except for one, in whom prenatal hydrocephalus is diagnosed. Patient body fluids show an elevation in N-acetyl-D-mannosamine levels, and patient-derived fibroblasts have reduced enzyme activity and are unable to incorporate sialic acid precursors into sialylated glycoproteins, phenotypes, overview |
739153 |
| 2.5.1.56 | malfunction |
knockdown of nansa in zebrafish embryos results in abnormal skeletal development, but with normal sialylation of plasma proteins, and exogenously added sialic acid partially rescues the skeletal phenotype |
739153 |
| 2.5.1.56 | metabolism |
formation of sialic acid or N-acetylneuraminic acid to produce a capsular polysacccharide of polysialic acid to evade the host's immune system by mimicking its own cell surface polysaccharides |
707514 |
| 2.5.1.56 | more |
a complex hydrogen-bonding relay links the roles of the catalytic and AFPL domains across subunit boundaries, analyzed by small angle X-ray scattering, molecular dynamics simulations, and amino acid substitutions, overview |
-, 739614 |
| 2.5.1.56 | more |
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 |
-, 737676 |
| 2.5.1.56 | physiological function |
enzyme-mediated synthesis of sialic acid is required for early brain development and skeletal growth |
739153 |
| 2.5.1.56 | physiological function |
key enzyme in microorganisms for producing N-acetylneuraminic acid through the irreversible condensation of N-acetylmannosamine and phosphoenolpyruvate |
-, 738339 |
| 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 |
-, 737676 |
