The amino acid sequence of tauropine dehydrogenase from the polychaete Arabella iricolor

Nobuhiro Kan-no, Noriyuki Endo, Shunsuke Moriyama, Eizoh Nagahisa, Minoru Sato

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

The amino acid sequence of tauropine dehydrogenase (EC 1.5.1.23) from the polychaete Arabella iricolor was determined by automated sequencing of fragments obtained by cleavage with lysyl endopeptidase, endoproteinase Glu-C, and cyanogen bromide. The purified enzyme contained two isoforms that differ only in the 41st amino acid residue (Thr or Ile). Although the sequence contained eight Cys residues, intrachain disulfide bonds were not found. Two possible N-linked glycosylation sites occur in the sequences, but the enzyme does not appear to contain bound carbohydrates. Based on these data, the two isoforms of Arabella tauropine dehydrogenase are simple proteins consisted of 396 amino acid residues with calculated molecular masses of 43,085.7 Da (Thr41 isoform) and 43,097.8 Da (Ile41 isoform).

Original languageEnglish
Pages (from-to)475-485
Number of pages11
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume140
Issue number3
DOIs
Publication statusPublished - 2005 Mar

Keywords

  • Amino acid sequence
  • Arabella iricolor
  • Disulfide bond
  • Invertebrate
  • Isoform
  • Opine dehydrogenase
  • Polychaete
  • Tauropine dehydrogenase

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology

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