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

    Research output: Contribution to journalArticlepeer-review

    15 Citations (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.

    Original languageEnglish
    Pages (from-to)331-339
    Number of pages9
    JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
    Issue number3
    Publication statusPublished - 2005 Jul


    • Amino acid sequence
    • Halichondria japonica
    • Mu-crystallin
    • Opine dehydrogenase
    • Ornithine cyclodeaminase
    • Sponge
    • Tauropine dehydrogenase
    • cDNA

    ASJC Scopus subject areas

    • Biochemistry
    • Physiology
    • Molecular Biology


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