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The hmd gene of histamine dehydrogenase from Nocardioides simplex was overexpressed in Escherichia coli, and the resulting enzyme was purified to homogeneity. The purified recombinant enzyme is almost identical with the native enzyme in view of molecular weight and specific activity, and is stoichiometrically assembled with the three cofactors 6-S-cysteinyl FMN, 4Fe-4S cluster, and ADP.

bioscience, biotechnology, and biochemistry

Production of Completely Flavinylated Histamine Dehydrogenase, Unique Covalently Bound Flavin, and Iron–Sulfur Cluster-Containing Enzyme of<i>Nocardioides simplex</i>in<i>Escherichia coli</i>, and Its Properties

Production of Completely Flavinylated Histamine Dehydrogenase, Unique Covalently Bound Flavin, and Iron–Sulfur Cluster-Containing Enzyme ofNocardioides simplexinEscherichia coli, and Its Properties