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Literature summary extracted from

  • Caldinelli, L.; Iametti, S.; Barbiroli, A.; Bonomi, F.; Fessas, D.; Molla, G.; Pilone, M.S.; Pollegioni, L.
    Dissecting the structural determinants of the stability of cholesterol oxidase containing covalently bound flavin (2005), J. Biol. Chem., 280, 22572-22581.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.6 H69A site-directed mutagenesis, the mutant does not bind FAD, the mutant is more sensitive to urea and unfolds at lower urea concentrations of 3 M compared to the wild-type enzyme at 5 M, the mutant also has a lower melting temperature Brevibacterium sterolicum

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.6 Brevibacterium sterolicum
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.1.3.6 unfolding and folding after urea treatment of wild-type enzyme and mutant H69A, equilibrium unfolding study, kinetics Brevibacterium sterolicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.6 cholesterol + O2
-
 Brevibacterium sterolicum cholest-4-en-3-one + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.3.6 monomer structural determinants of the enzymes' stability Brevibacterium sterolicum

Synonyms

EC Number Synonyms Comment Organism
1.1.3.6 CO
-
 Brevibacterium sterolicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.6 25
-
 assay at Brevibacterium sterolicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.6 7.5
-
 assay at Brevibacterium sterolicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.6 FAD flavoenzyme, FAD is covalently linked to His69 Brevibacterium sterolicum