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Literature summary for 1.7.3.3 extracted from

  • Caves, M.S.; Derham, B.K.; Jezek, J.; Freedman, R.B.
    Thermal inactivation of uricase (urate oxidase): mechanism and effects of additives (2013), Biochemistry, 52, 497-507.
    View publication on PubMed
Search for more literature for 1.7.3.3

Activating Compound

Activating Compound Comment Organism Structure
additional information dithiothreitol treatment leads to an insignificant change in specific activity below 1% Candida sp. (in: Saccharomycetales)

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Candida sp. (in: Saccharomycetales)

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
 4 * 36000, SDS-PAGE Candida sp. (in: Saccharomycetales)
140000
-
 gel filtration Candida sp. (in: Saccharomycetales)

Organism

Organism UniProt Comment Textmining
Candida sp. (in: Saccharomycetales)
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Candida sp. (in: Saccharomycetales)
-

Subunits

Subunits Comment Organism
tetramer 4 * 36000, SDS-PAGE Candida sp. (in: Saccharomycetales)

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the main phase of thermal inactivation follows an irreversible two-state mechanism, with loss of about 20% of the helical structure, loss of the majority of the tertiary structure, and partial exposure of tryptophan residues to solution being approximately concurrent with activity loss. This process results in the formation of aggregated molten globules. In addition, a rapid reversible denaturation phase occurs that is not completely coupled to the main phase. Enzyme inactivation is inhibited by the presence of glycerol and trimethylamine oxide. NaCl destabilizes the enzyme at elevated temperature Candida sp. (in: Saccharomycetales)