Abstract
A procedure is described for the identification of the covalently-bound organic cofactor in copper-containing amine oxidases. Reaction of these enzymes with a suitable hydrazine gave a cofactor adduct stable against attack by nucleophilic amino acids released upon protein degradation. Proteolysis detached the adduct from the protein chain, enabling its isolation and comparison with the model compound prepared from the hydrazine and free PQQ (pyrrolo-quinoline quinone). The comparison showed that bovine serum amine oxidase, diamine oxidase from porcine kidney, lysyl oxidase from human placenta, and methylamine oxidase from the bacterium Arthrobacter PI, all contain one PQQ per enzyme molecule. The finding opens new avenues for further research on the mechanism and role of this type of amine oxidases and the significance of PQQ for mammalian organisms.
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