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Literature summary for 3.1.1.53 extracted from

  • Song, L.; Zhou, H.; Cai, X.; Li, C.; Liang, J.; Jin, C.
    NeuA O-acetylesterase activity is specific for CMP-activated O-acetyl sialic acid in Streptococcus suis serotype 2 (2011), Biochem. Biophys. Res. Commun., 410, 212-217.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
CTP activates Streptococcus suis

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli BL21(DE3). SsneuA can restore both CMP-Neu5Ac synthetase and O-acetylesterase activities in complemented enzyme-deficient Escherichia coli strains, but the activities in the complemented strain are different from those in the wild-type Escherichia coli strain. However, the Streptococcus suis O-acetylesterase domain alone is unable to act on intracellular O-acetyl-Neu5Ac in Escherichia coli Streptococcus suis

Protein Variants

Protein Variants Comment Organism
additional information the mutant SsNeuAs truncated from 166 to 233 amino acids at the N-terminal a re active for pNP-Ac and their esterase activities are almost the same as the wild-type, only with one exception of the SsNeuA167-410, while the mutant SsNeuAs terminated at amino acid position of 227, 232, 233, 241, 247, 267, 283, 293, 312, 322, 338, 355 and 377 are inactive in CMP-Neu5Ac synthetase activity, even removal of 33 amino acid residues at C-terminal of the SsNeuA leads to a complete loss of CMP-Neu5Ac synthetase activity Streptococcus suis
S258A site-directed mutagenesis Streptococcus suis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Streptococcus suis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CMP-O9-acetyl-N-acetylneuraminate + H2O Streptococcus suis SsNeuA is a bifunctional CMP-Neu5Ac synthetase/O-acetylesterase, which strictly de-O-acetylates CMP-O-acetyl-Neu5Ac CMP-N-acetylneuraminate + acetate
-
?

Organism

Organism UniProt Comment Textmining
Streptococcus suis
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serotype 2
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8
-
purified recombinant 29 kDa O-acetylesterase fragment, pH 7.2, 37°C Streptococcus suis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl acetate + H2O
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Streptococcus suis 4-nitrophenol + acetate
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?
CMP-O9-acetyl-N-acetylneuraminate + H2O SsNeuA is a bifunctional CMP-Neu5Ac synthetase/O-acetylesterase, which strictly de-O-acetylates CMP-O-acetyl-Neu5Ac Streptococcus suis CMP-N-acetylneuraminate + acetate
-
?

Subunits

Subunits Comment Organism
More SsNeuA is cleaved into two fragments, in which the 29-kDa protein recovers from SDS-PAGE still remaining its O-acetylesterase activity. The esterase domain is composed of 177 amino acid residues at C-terminal of the SsNeuA and its activity does not structurally depend on the CMP-Neu5Ac synthetase domain, overview Streptococcus suis

Synonyms

Synonyms Comment Organism
SsNeuA
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Streptococcus suis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
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substrate 4-nitrophenyl acetate, wild-type SsNeuA and mutant SsNeuA234-410 Streptococcus suis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 8.5 substrate 4-nitrophenyl acetate, wild-type SsNeuA and mutant SsNeuA234-410 Streptococcus suis

General Information

General Information Comment Organism
additional information SsNeuAc contains a asignature consensus sequence for serine esterase, Gly-Xaa-Ser-Xaa-Gly, is found within the C-terminal half Streptococcus suis
physiological function the O-acetylesterase is probably essential for the synthesis of capsular Neu5Ac in Streptococcus suis Streptococcus suis