Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.43 extracted from

  • Yu, H.; Ryan, W.; Yu, H.; Chen, X.
    Characterization of a bifunctional cytidine 5-monophosphate N-acetylneuraminic acid synthetase cloned from Streptococcus agalactiae (2006), Biotechnol. Lett., 28, 107-113.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information DTT has no effect on enzyme activity Streptococcus agalactiae

Cloned(Commentary)

Cloned (Comment) Organism
cloned in Escherichia coli as a His6-tagged fusion protein Streptococcus agalactiae

Protein Variants

Protein Variants Comment Organism
additional information amino acid sequence alignment of SaV CSS indicate that the C-terminus belongs to the newly discovered SGNH-hydrolase subfamily of serine esterases/lipases Streptococcus agalactiae

Inhibitors

Inhibitors Comment Organism Structure
EDTA enzyme is inactive in the presence of 5 mM EDTA Streptococcus agalactiae
Mn2+ both catalytic functions are impaired by high concentrations of Mn2+ Streptococcus agalactiae
additional information no activity is detected when the enzyme is substituted with 5-35 mM Co2+ or Ca2+ Streptococcus agalactiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.35
-
N-glycolylneuraminic acid
-
Streptococcus agalactiae
0.62
-
deaminoneuraminic acid
-
Streptococcus agalactiae
0.96
-
CTP
-
Streptococcus agalactiae
5.6
-
Neu5Ac
-
Streptococcus agalactiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for CMP-sialic acid synthetase activity but not for acetylhydrolase activity Streptococcus agalactiae
Mn2+ required for CMP-sialic acid synthetase activity but not for acetylhydrolase activity, maximum activity with 4 mM MnCl Streptococcus agalactiae

Organism

Organism UniProt Comment Textmining
Streptococcus agalactiae Q9AFG9 serotype V strain2603 V/R
-

Purification (Commentary)

Purification (Comment) Organism
C-His6-tagged CSS is purified using a nickel-nitrilotriacetic acid-agarose (Ni2+-NTA-agarose) affinity column Streptococcus agalactiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deaminoneuraminic acid + CTP N-glycolylneuraminic acid (Neu5Gc) and deaminoneuraminic acid (KDN) are also substrates Streptococcus agalactiae CMP-KDN + diphosphate
-
?
additional information SaV CSS is a bifunctional enzyme having both CMP-sialic acid synthetase and acetylhydrolase (acylesterase) activities Streptococcus agalactiae ?
-
?
N-acetylneuraminic acid + CTP N-glycolylneuraminic acid (Neu5Gc) and deaminoneuraminic acid (KDN) are also substrates Streptococcus agalactiae CMP-Neu5Ac + diphosphate
-
?
N-glycolylneuraminic acid + CTP N-glycolylneuraminic acid (Neu5Gc) and deaminoneuraminic acid (KDN) are also substrates Streptococcus agalactiae CMP-Neu5Gc + diphosphate
-
?

Synonyms

Synonyms Comment Organism
CMP-sialic acid synthetase (CSS)
-
Streptococcus agalactiae
cytidine 5-monophosphate N-acetylneuraminic acid synthetase
-
Streptococcus agalactiae
SaV CSS
-
Streptococcus agalactiae
sialic acid cytidylyltransferase
-
Streptococcus agalactiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Streptococcus agalactiae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
enzyme is more stable at lower temperatures, 55% of enzyme activity remains after 24 h incubation at 25°C Streptococcus agalactiae
37
-
enzyme is not stable at 37°C, incubation for 1 h decreases enzyme activity by 50%, incubation for 24 h at 37°C completely inactivates enzyme activity Streptococcus agalactiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.067
-
deaminoneuraminic acid
-
Streptococcus agalactiae
0.68
-
N-glycolylneuraminic acid
-
Streptococcus agalactiae
14
-
CTP
-
Streptococcus agalactiae
16
-
Neu5Ac
-
Streptococcus agalactiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
optimal CMP-sialic acid synthetase activity Streptococcus agalactiae

pH Range

pH Minimum pH Maximum Comment Organism
7.5 10.5 enzyme is active in a wide pH-range Streptococcus agalactiae