Structure and properties of the recombinant NADH-cytochrome b5 reductase of Physarum polycephalum.

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Ikegami T, Kameyama E, Yamamoto SY, Minami Y, Yubisui T

Structure and properties of the recombinant NADH-cytochrome b5 reductase of Physarum polycephalum.

Biosci Biotechnol Biochem. 2007 Mar;71(3):783-90. Epub 2007 Mar 7.

PubMed ID

17341833 [ View in PubMed

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Abstract

A cDNA for NADH-cytochrome b(5) reductase of Physarum polycephalum was cloned from a cDNA library, and the nucleotide sequence of the cDNA was determined (accession no. AB259870). The DNA of 943 base pairs contains 5'- and 3'-noncoding sequences, including a polyadenylation sequence, and a coding sequence of 843 base pairs. The amino acid sequence (281 residues) deduced from the nucleotide sequence was 25 residues shorter than those of vertebrate enzymes. Nevertheless, the recombinant Physarum enzyme showed enzyme activity comparable to that of the human enzyme. The recombinant Physarum enzyme showed a pH optimum of around 6.0, and apparent K(m) values of 2 microM and 14 microM for NADH and cytochrome b(5) respectively. The purified recombinant enzyme showed a typical FAD-derived absorption peak of cytochrome b(5) reductase at around 460 nm, with a shoulder at 480 nm. These results suggest that the Physarum enzyme plays an important role in the organism.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
NADH	NADH-cytochrome b5 reductase 3	Protein	Humans	Unknown	Not Available	Details