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

Nobutaka Fujieda | Zendy; Noriaki Tsuse | Zendy; Atsuko Satoh | Zendy; Tokuji Ikeda | Zendy; Kenji Kano | Zendy

Open Access

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

Author(s) -

Nobutaka Fujieda,

Noriaki Tsuse,

Atsuko Satoh,

Tokuji Ikeda,

Kenji Kano

Publication year - 2005

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.69.2459

Subject(s) - escherichia coli , enzyme , biochemistry , cofactor , flavin group , dehydrogenase , chemistry , flavin adenine dinucleotide , stereochemistry , covalent bond , biology , gene , organic chemistry

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.

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