Characterization of cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: European Journal of Biochemistry ; 250 (1997), 2. - S. 369-376. - ISSN 0014-2956. - eISSN 1432-1033
- Classification
-
Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
-
Bibliothek der Universität Konstanz
- (when)
-
2008
- Creator
-
Gadda, Giovanni
Wels, Gaby
Pollegioni, Loredano
Zucchelli, Silvia
Ambrosius, Dorothea
Pilone, Mirella S.
Ghisla, Sandro
- URN
-
urn:nbn:de:bsz:352-opus-52306
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:57 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Gadda, Giovanni
- Wels, Gaby
- Pollegioni, Loredano
- Zucchelli, Silvia
- Ambrosius, Dorothea
- Pilone, Mirella S.
- Ghisla, Sandro
- Bibliothek der Universität Konstanz
Time of origin
- 2008
Other Objects (12)
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Cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum : effect of surfactants and organic solvents on activity
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Cholesterol oxidase from Brevibacterium sterolicum : the relationship between covalent flavinylation and redox properties
Studies on the mechanism of action of the flavoenzyme lactate oxidase : proton uptake and release during the binding of transition state analogs
Structural and kinetic analyses of the H121A mutant of cholesterol oxidase
Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair
Kinetic mechanisms of cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum
Cholesterol oxidase from Brevibacterium sterolicum and Streptomyces hygroscopicus : a covalent FAD binding vs. a non-covalent one
L-Lactate oxidase
Cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum : effect of surfactants and organic solvents on activity
Synthesis of the Flavocoenzyme of Monoamine Oxidase
Mechanism of Inactivation of the Flavoenzyme Lactate Oxidase by Oxalate
Studies on Glycollate Oxidase from Pea Leaves : Determination of Stereospecificity and Mode of Inhibition by alpha-Hydroxybutynoate
Studies on the catalytic mechanism of lactate oxidase : formation of enantiometric flavin-N(5)-glycollyl adducts via carbanion intermediates
Cholesterol oxidase from Brevibacterium sterolicum : the relationship between covalent flavinylation and redox properties
Studies on the mechanism of action of the flavoenzyme lactate oxidase : proton uptake and release during the binding of transition state analogs
Structural and kinetic analyses of the H121A mutant of cholesterol oxidase
Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair
Kinetic mechanisms of cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum
Cholesterol oxidase from Brevibacterium sterolicum and Streptomyces hygroscopicus : a covalent FAD binding vs. a non-covalent one
L-Lactate oxidase
Cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum : effect of surfactants and organic solvents on activity
Synthesis of the Flavocoenzyme of Monoamine Oxidase
Mechanism of Inactivation of the Flavoenzyme Lactate Oxidase by Oxalate
Studies on Glycollate Oxidase from Pea Leaves : Determination of Stereospecificity and Mode of Inhibition by alpha-Hydroxybutynoate
Studies on the catalytic mechanism of lactate oxidase : formation of enantiometric flavin-N(5)-glycollyl adducts via carbanion intermediates
Cholesterol oxidase from Brevibacterium sterolicum : the relationship between covalent flavinylation and redox properties
Studies on the mechanism of action of the flavoenzyme lactate oxidase : proton uptake and release during the binding of transition state analogs
Structural and kinetic analyses of the H121A mutant of cholesterol oxidase