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 …

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 …

The network‐forming attributes of gluten have been investigated for decades, but no study
has comprehensively addressed the differences in gluten network evolution between strong …

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 …

Structural changes ensuing from denaturation of soy proteins in solution or occurring at the
oil–water interface were studied by fluorescence spectroscopy. Studies were carried out on …

Correlated mutation analyses (CMA) on multiple sequence alignments are widely used for
the prediction of the function of amino acids. The accuracy of CMA‐based predictions is …

Flavoenzymes are versatile biocatalysts with extraordinary properties. They are not only vital
to life by orchestrating complex transformations in biological processes but offer numerous …

Cholesterol oxidase (CHOx), a FAD-dependent enzyme of the oxido-reductase family
catalyzes the oxidation of cholesterol to cholestenone. CHOx is produced by a large number …

Here, we have demonstrated an easy and efficient synthetic route for the synthesis of the
flavo-peptide conjugates as model for the naturally occurring covalently linked …

Due to their early origin and extreme conservation, cofactors are valuable molecular fossils
for tracing the origin and evolution of proteins. First, as the order of protein folds binding with …