The semicarbazide-sensitive amine oxidases constitute a group of copper-containing enzymes whose physiological function is unclear. The enzymes are present in various tissues, including blood plasma. At present, the source of the plasma enzyme in humans is not known. Results of a recent study suggested that semicarbazide-sensitive amine oxidase is expressed in the skeleton, e.g. in the spine. U...

Abstract Activity‐based protein profiling (ABPP) as a proteomic tool allows measuring the activity of enzyme classes or distinct proteins in their cellular context, annotating function uncharacterized proteins, and investigating target profile small molecule inhibitors. While hydrolases other classes, which exhibit characteristic nucleophilic residue, can be addressed by electrophilic activity‐...

Reductive activation of O2 by glucose oxidase and by copper amine oxidases (and also by tyrosine hydroxylase and lypoxygenase) illustrate very interesting spin chemistry. The rate-determining step in these processes is connected with electron transfer from reduced cofactor (E) to O2 and is, in fact, the triplet –> singlet intersystem crossing (ISC) at the stage of the radical pair O2 − . . . E+...

Although this human plasma enzyme was shown (1) to have certain characteristics in common with plasma amine oxidases from other mammals (2-6), it could be distinguished from these other plasma enzymes by its substrate specificity. During studies relating to the substrate specificity of the human enzyme, the oxidation of aliphatic amines was noted to have a number of distinctive kinetic features...

The lysyl oxidase-like protein 4 (LOXL4) is the latest member of the emerging family of lysyl oxidases, several of which were shown to function as copper-dependent amine oxidases catalyzing lysine-derived cross-links in extracellular matrix proteins. LOXL4 contains four scavenger receptor cysteine-rich domains in addition to the characteristic domains of the LOX family, including the copper-bin...