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Literature summary for 1.1.3.6 extracted from

  • Piubelli, L.; Pedotti, M.; Molla, G.; Feindler-Boeckh, S.; Ghisla, S.; Pilone, M.S.; Pollegioni, L.
    On the oxygen reactivity of flavoprotein oxidases: An oxygen access tunnel and gate in Brevibacterium sterolicum cholesterol oxidase (2008), J. Biol. Chem., 283, 24738-24747.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.3.6

Cloned(Commentary)

Cloned (Comment) Organism
-
 Brevibacterium sterolicum

Protein Variants

Protein Variants Comment Organism
E311D mutations of Glu311 cause a switch in the basic kinetic mechanism of the reaction of reduced cholesterol oxidase with dioxygen: wild-type cholesterol oxidase shows a saturation behavior with increasing oxygen concentration, while for Glu311 mutants a linear dependence is found that is assumed to reflect a simple second order process Brevibacterium sterolicum
E311L mutations of Glu311 cause a switch in the basic kinetic mechanism of the reaction of reduced cholesterol oxidase with dioxygen: wild-type cholesterol oxidase shows a saturation behavior with increasing oxygen concentration, while for Glu311 mutants a linear dependence is found that is assumed to reflect a simple second order process Brevibacterium sterolicum
E311Q mutations of Glu311 cause a switch in the basic kinetic mechanism of the reaction of reduced cholesterol oxidase with dioxygen: wild-type cholesterol oxidase shows a saturation behavior with increasing oxygen concentration, while for Glu311 mutants a linear dependence is found that is assumed to reflect a simple second order process Brevibacterium sterolicum

Organism

Organism UniProt Comment Textmining
Brevibacterium sterolicum
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-
-

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Brevibacterium sterolicum