1,721,030 research outputs found
pH and kinetic isotope effects in D-amino acid oxidase catalysis - Evidence for a concerted mechanism in substrate dehydrogenation via hydride transfer
No full textOn the mechanism of D-amino acid oxidase. Structure/linear free energy correlations and deuterium kinetic isotope effects using p-substituted phenylglycines
No full textCholesterol oxidase from Brevibacterium sterolicum and Streptomices hygroscopicus: a covalent FAD binding vs. a non-covalent one
No full textCholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum: effect of surfactants and organic solvents on activity
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Investigating the role of flavin covalent attachment: the case of cholesterol oxidase from Brevibacterium sterolicum
No full textIdentification and role of ionizing functional groups at the active center of Rhodotorula gracilis D-amino acids oxidase
No full textD-Amino acid oxidase (DAAO) is a flavoprotein oxidase that catalyzes the oxidation of amino acids and produces ketoacids and H2O2. The rate of product release from reduced DAAO from Rhodotorula gracilis is pH dependent and reflects a pKa of ∼9.3. Binding of benzoate and 3,3,3-trifluoro-D-alanine to wild-type and Y238F-DAAO is also pH dependent (pKa = 9.8 ± 0.1 and 9.05 ± 0.1, respectively for benzoate binding). However, binding of benzoate to Y223F-DAAO is pH independent, indicating the pKa is due to Y223-OH. This latter residue is thus involved in substrate binding, and probably is the group that governs product release. In contrast to this, the second active site tyrosine, Y238, has little influence on ligand binding. © 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved
Cholesterol oxidase from Brevibacterium sterolicum - The relationship between covalent flavinylation and redox properties
No full textCholesterol oxidase from Brevibacterium sterolicum and Streptomyces hygroscopicus: a covalent FAD binding vs. a non-covalent one
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