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Literature summary for 2.5.1.47 extracted from

  • Kuske, C.R.; Ticknor, L.O.; Guzman, E.; Gurley, L.R.; Valdez, J.G.; Thompson, M.E.; Jackson, P.J.
    Purification and characterization of O-acetylserine sulfhydrylase isoenzymes from Datura innoxia (1994), J. Biol. Chem., 269, 6223-6232.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Sulfide above 200 mM Datura inoxia

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information no Michaelis-Menten-kinetics Datura inoxia

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31200
-
1 * 32000 + 1 * 31200, isoenzyme 2, SDS-PAGE Datura inoxia
32000
-
2 * 32000, isoenzymes 1 and 3, SDS-PAGE Datura inoxia
32000
-
1 * 32000 + 1 * 31200, isoenzyme 2, SDS-PAGE Datura inoxia
63000
-
isoenzymes one and three, gel filtration Datura inoxia
86000
-
isoenzyme 2, gel filtration Datura inoxia

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
O-acetyl-L-Ser + sulfide Datura inoxia involved in glutathione formation L-Cys + acetate
-
?

Organism

Organism UniProt Comment Textmining
Datura inoxia
-
three isoenzymes
-

Purification (Commentary)

Purification (Comment) Organism
-
Datura inoxia

Source Tissue

Source Tissue Comment Organism Textmining
cell suspension culture
-
Datura inoxia
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
880
-
isoenzyme 1 and 2 Datura inoxia

Storage Stability

Storage Stability Organism
-70°C, Tris-HCl, pH 8.1, glycerol, 6 months, no loss of activity Datura inoxia

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-acetyl-L-Ser + sulfide involved in glutathione formation Datura inoxia L-Cys + acetate
-
?

Subunits

Subunits Comment Organism
dimer 2 * 32000, isoenzymes 1 and 3, SDS-PAGE Datura inoxia
dimer 1 * 32000 + 1 * 31200, isoenzyme 2, SDS-PAGE Datura inoxia
More amino acid composition Datura inoxia

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
42 58 all isoenzymes Datura inoxia

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
all isoenzymes Datura inoxia

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate responsible for O-acetylserine binding Datura inoxia