EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.5.1.56 | by small angle X-ray scattering and structure analysis, PDB ID 1XUZ | Neisseria meningitidis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.5.1.56 | E134A | site-directed mutagenesis | Neisseria meningitidis |
2.5.1.56 | E282A | site-directed mutagenesis | Neisseria meningitidis |
2.5.1.56 | E282A/T285A | site-directed mutagenesis | Neisseria meningitidis |
2.5.1.56 | additional information | generation of a truncated variant of enzyme NANAS which lacks the C-terminal AFPL domain, G272Term by inserting a stop codon. The truncation is made at residue Gly272 prior to the linker region | Neisseria meningitidis |
2.5.1.56 | T285A | site-directed mutagenesis | Neisseria meningitidis |
2.5.1.56 | T285F | site-directed mutagenesis | Neisseria meningitidis |
EC Number | General Stability | Organism |
---|---|---|
2.5.1.56 | phosphoenolpyruvate has a major effect on the thermal stability of the wild-type enzyme requiring the C-terminal AFPL domain | Neisseria meningitidis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.56 | additional information | - |
additional information | kinetic analysis of wild-ype and mutant enzymes, no kinetic activity can be observed for mutant G272Term with phosphoenolpyruvate, binding constants for wild-type, overview | Neisseria meningitidis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.5.1.56 | Mn2+ | required, increases the enzyme stability, binding of Mn2+ is associated with a change in the average conformation of enzyme NmeNANAS | Neisseria meningitidis |
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 | additional information | 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 | additional information | 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 | 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 | homodimer | the enzyme comprises two distinct domains, an N-terminal catalytic (beta/alpha)8 barrel linked to a C-terminal antifreeze protein-like (AFPL) domain. Loss of the AFPL domain destabilizes the dimeric form of the enzyme nd renders it inactive. The AFPL domain plays a critical role for both the catalytic function and quaternary structure stability of N-acetylneuraminic acid synthase. The enzyme mutant G272Term lacking the AFPL domain is partly monomeric | Neisseria meningitidis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.56 | NANAS | - |
Neisseria meningitidis |
2.5.1.56 | NmeNANAS | - |
Neisseria meningitidis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.5.1.56 | additional information | - |
the wild-type apoenzyme has a higher melting temperature of 42.6°C compared to the mutant G272Term apoenzyme with 36.5°C. Unlike the wild-type enzyme, the melting temperature of mutant G272Term in the presence of Mn2+ remains consistent and is not influenced by the addition of different ligand combinations. The melting temperature of wild-type NmeNANAS increases slightly in the presence of Mn2+ | Neisseria meningitidis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.5.1.56 | 7.5 | - |
assay at | Neisseria meningitidis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
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 | Neisseria meningitidis |
2.5.1.56 | additional information | 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 | Neisseria meningitidis |