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

BRENDA support

Literature summary for 2.5.1.47 extracted from

  • Mino, K.; Yamanoue, T.; Sakiyama, T.; Eisaki, N.; Matsuyama, A.; Nakanishi, K.
    Effects of bienzyme complex formation of cysteine synthetase from Escherichia coli on some properties and kinetics (2000), Biosci. Biotechnol. Biochem., 64, 1628-1640.
    View publication on PubMed
Search for more literature for 2.5.1.47

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol slight activation Escherichia coli
iodoacetamide slight activation Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
(NH4)6Mo7O24 1 mM, 97% inhibition Escherichia coli
acetate
-
 Escherichia coli
AgNO3 1 mM, 22% inhibition Escherichia coli
Cys
-
 Escherichia coli
EDTA 1 mM, 16% inhibition Escherichia coli
FeSO4 1 mM, 96% inhibition Escherichia coli
O-acetylserine
-
 Escherichia coli
p-chloromercuribenzoate 1 mM, 59% inhibition Escherichia coli
S2-
-
 Escherichia coli
Sulfide
-
 Escherichia coli
Zn2+ 1 mM, 94% inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.006
-
 H2S pH 7.5, 25°C, free enzyme Escherichia coli
0.013
-
 H2S pH 7.5, 25°C, enzyme bound to serine acetyltransferase Escherichia coli
4.8
-
 O-acetyl-L-Ser pH 7.5, 25°C, free enzyme Escherichia coli
27
-
 O-acetyl-L-Ser pH 7.5, 25°C, enzyme bound to serine acetyltransferase Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ slight activation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information activity of the enzyme bound to serine acetyltransferase is lower than that of the free enzyme Escherichia coli ?
-
 ?
O-acetyl-L-Ser + H2S
-
 Escherichia coli L-Cys + acetate
-
 ?
O-acetyl-L-serine
-
 Escherichia coli L-cysteine + acetate
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-
-
 12 h, about 20% loss of activity Escherichia coli
20 40 12 h, stable Escherichia coli
60
-
 12 h, about 15% loss of activity Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9 free enzyme Escherichia coli
9.5
-
 enzyme bound to serine acetyltransferase Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.011
-
 S2- pH 7.5, 25 C, free enzyme Escherichia coli
0.11
-
 S2- pH 7.5, 25 C, enzyme bound to serine acetyltransferase Escherichia coli
7.1
-
 O-acetyl-L-Ser pH 7.5, 25 C, free enzyme Escherichia coli
8.6
-
 cysteine pH 7.5, 25 C, free enzyme Escherichia coli
18
-
 O-acetyl-L-Ser pH 7.5, 25 C, enzyme bound to serine acetyltransferase Escherichia coli
48
-
 cysteine pH 7.5, 25 C, enzyme bound to serine acetyltransferase Escherichia coli
160
-
 acetate pH 7.5, 25 C, free enzyme Escherichia coli
340
-
 acetate pH 7.5, 25 C, enzyme bound to serine acetyltransferase Escherichia coli