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    Biochem Biophys Res Commun. 1993 Dec 30;197(3):1518-23.

    Complete amino acid sequence of biliverdin-IX beta reductase from human liver.

    Yamaguchi T, Komuro A, Nakano Y, Tomita M, Nakajima H.

    Department of Biochemical Genetics, Tokyo Medical and Dental University, Japan.

    The amino acid sequence of biliverdin-IX beta reductase (EC1.3.1.24) from human liver was determined by automated Edman degradation of peptides generated by enzymatic and chemical cleavages. The enzyme was a single polypeptide chain of 204 amino acid residues, and its amino acid sequence had no significant homology to that of rat liver biliverdin-IX alpha reductase. Biliverdin-IX alpha reductase from human liver had intense homology to the rat enzyme. Cysteinyl residues are essential for the enzymatic activity of biliverdin-IX alpha, but nonessential for that of biliverdin-IX beta reductase. The results strongly indicate that the two enzymes, biliverdin-IX alpha reductase and biliverdin-IX beta reductase, are distinct in enzymatic action mechanisms as well as ancient origins of gene.

    PMID: 8280170 [PubMed - indexed for MEDLINE]

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