Over time, organisms have evolved strategies to cope with the abundance of dioxygen on
Earth. Oxygen-utilizing enzymes tightly control the reactions involving O2 mostly by …

Biosensors have recently gained much attention in the field of health care for the
management of various important analytes in a biological system. The area achieved …

Many enzymes use one or more cofactors, such as biotin, heme, or flavin. These cofactors
may be bound to the enzyme in a noncovalent or covalent manner. Although most …

Abstract Alcohol oxidases (Alcohol: O 2 Oxidoreductase; EC 1.1. 3. x) are flavoenzymes that
catalyze the oxidation of alcohols to the corresponding carbonyl compounds with a …

Cholesterol oxidases are bifunctional flavoenzymes that catalyze the oxidation of steroid
substrates which have a hydroxyl group at the 3β position of the steroid ring system. The …

Cholesterol oxidase is a bacterial FAD‐containing flavooxidase that catalyzes the first
reaction in cholesterol catabolism. Indeed, this enzyme catalyzes two reactions: the …

Most flavin-dependent enzymes contain a dissociable flavin cofactor. We present a new
approach for installing in vivo a covalent bond between a flavin cofactor and its host protein …

Microbial cholesterol oxidase is an enzyme of great commercial value, widely employed by
laboratories routinely devoted to the determination of cholesterol concentrations in serum …

Cholesterol was first found in gallstones as an animal sterol; hence it is called cholesterol.
Cholesterol oxidase is the chief enzyme in the process of cholesterol degradation. Its role is …

Glycine oxidase from Bacillus subtilis is a homotetrameric flavoprotein of great potential
biotechnological use because it catalyzes the oxidative deamination of various amines and …