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

BRENDA support

Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.5.1.47 dithiothreitol slight activation Escherichia coli
2.5.1.47 iodoacetamide slight activation Escherichia coli

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.47 0.006
-
 H2S pH 7.5, 25°C, free enzyme Escherichia coli
2.5.1.47 0.013
-
 H2S pH 7.5, 25°C, enzyme bound to serine acetyltransferase Escherichia coli
2.5.1.47 4.8
-
 O-acetyl-L-Ser pH 7.5, 25°C, free enzyme Escherichia coli
2.5.1.47 27
-
 O-acetyl-L-Ser pH 7.5, 25°C, enzyme bound to serine acetyltransferase Escherichia coli

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.47 Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.5.1.47
-
-
 12 h, about 20% loss of activity Escherichia coli
2.5.1.47 20 40 12 h, stable Escherichia coli
2.5.1.47 60
-
 12 h, about 15% loss of activity Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.47 8 9 free enzyme Escherichia coli
2.5.1.47 9.5
-
 enzyme bound to serine acetyltransferase Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.5.1.47 0.011
-
 S2- pH 7.5, 25 C, free enzyme Escherichia coli
2.5.1.47 0.11
-
 S2- pH 7.5, 25 C, enzyme bound to serine acetyltransferase Escherichia coli
2.5.1.47 7.1
-
 O-acetyl-L-Ser pH 7.5, 25 C, free enzyme Escherichia coli
2.5.1.47 8.6
-
 cysteine pH 7.5, 25 C, free enzyme Escherichia coli
2.5.1.47 18
-
 O-acetyl-L-Ser pH 7.5, 25 C, enzyme bound to serine acetyltransferase Escherichia coli
2.5.1.47 48
-
 cysteine pH 7.5, 25 C, enzyme bound to serine acetyltransferase Escherichia coli
2.5.1.47 160
-
 acetate pH 7.5, 25 C, free enzyme Escherichia coli
2.5.1.47 340
-
 acetate pH 7.5, 25 C, enzyme bound to serine acetyltransferase Escherichia coli