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Literature summary for 1.4.3.2 extracted from

  • Wellner, D.; Meister, A.
    Crystalline L-amino acid oxidase of Crotalus adamanteus (1960), J. Biol. Chem., 235, 2013-2018.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Crotalus adamanteus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
128000 153000 approach to equilibrium method Crotalus adamanteus
130000
-
-
Crotalus adamanteus

Organism

Organism UniProt Comment Textmining
Crotalus adamanteus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Crotalus adamanteus

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
Crotalus adamanteus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-amino acid + H2O + O2
-
Crotalus adamanteus 2-oxo acid + NH3 + H2O2
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
reduced form of the enzyme is much more stable to heat than oxidized form, substrates: e.g. L-Leu, L-Phe, L-Met protect from heat denaturation, no protection by D-leucine and L-lysine Crotalus adamanteus
73
-
no loss of activity after 5 min, heat-stable in presence of 0.01 mM L-leucine Crotalus adamanteus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Crotalus adamanteus

Cofactor

Cofactor Comment Organism Structure
FAD 2 mol of FAD per mol of enzyme Crotalus adamanteus