The amino acid sequence of tauropine dehydrogenase from the polychaete Arabella iricolor |
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Authors: | Kan-no Nobuhiro Endo Noriyuki Moriyama Shunsuke Nagahisa Eizoh Sato Minoru |
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Institution: | Department of Marine Biosciences, School of Fisheries Sciences, Kitasato University, Sanriku 160-4, Ohfunato, Iwate 022-0101, Japan. kan-no@kitasato-u.ac.jp |
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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). |
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