Tauropine dehydrogenase from the marine sponge Halichondria japonica is a homolog of ornithine cyclodeaminase/mu-crystallin

Nobuhiro Kan-No, Hiroto Matsu-Ura, Shinya Jikihara, Takayuki Yamamoto, Noriyuki Endo, Shunsuke Moriyama, Eizoh Nagahisa, Minoru Sato

    研究成果: Article査読

    15 被引用数 (Scopus)


    The partial amino acid sequence including the N- and C-terminal portions of tauropine dehydrogenase (EC from the marine sponge Halichondria japonica was determined by enzymatic cleavages followed by peptide sequencing. This information was used to design degenerate primers for amplification of cDNA encoding the tauropine dehydrogenase. The cDNA included 1231 nucleotides with an open reading frame of 1002 nucleotides that encodes a protein of 334 amino acid residues. From the peptide and nucleotide sequencing, the mature tauropine dehydrogenase was estimated to consist of 333 amino acid residues with an acetylated N-terminal serine residue and no intrachain disulfide bonds. The primary structure of the H. japonica enzyme showed apparent similarity with a homolog of ornithine cyclodeaminase from Rhizobium meliloti and other proteins of the ornithine cyclodeaminase/mu-crystallin family, but it showed no significant similarity with the known sequences of octopine dehydrogenases and tauropine dehydrogenases from marine invertebrates. These findings indicate that opine dehydrogenases in marine invertebrates are not all homologous.

    ジャーナルComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
    出版ステータスPublished - 2005 7月

    ASJC Scopus subject areas

    • 生化学
    • 生理学
    • 分子生物学


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