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Literature summary for 1.13.11.19 extracted from

  • Cavallini, D.; De Marco, C.; Scandurra, R.; Dupre, S.; Graziani, M.T.
    The enzymatic oxidation of cysteamine to hypotaurine. Purification and properties of the enzyme (1966), J. Biol. Chem., 241, 3189-3196.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
hydroxylamine cofactor-like compound Equus caballus
methylene blue cofactor-like compound Equus caballus
Se cofactor-like compound Equus caballus
Sulfide cofactor-like compound Equus caballus
sulfur cofactor-like compound Equus caballus

General Stability

General Stability Organism
exhaustive dialysis against water: partial denaturation, dialysis against water brought to pH 7.5 with concentrated ammonia or against 0.01 M potassium phosphate buffer, pH 7.6, has no effect Equus caballus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe 1 atom of nonheme iron per molecule of enzyme Equus caballus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
83000
-
sedimentation-diffusion equilibrium method Equus caballus

Organism

Organism UniProt Comment Textmining
Equus caballus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Equus caballus

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Equus caballus
-

Storage Stability

Storage Stability Organism
0°C, 70% saturated ammonium sulfate, stable for months Equus caballus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cysteamine + O2
-
Equus caballus hypotaurine
-
?
additional information specific for cysteamine Equus caballus additional information
-
?