TY - JOUR
T1 - Tauropine dehydrogenase from the marine sponge Halichondria japonica is a homolog of ornithine cyclodeaminase/mu-crystallin
AU - Kan-No, Nobuhiro
AU - Matsu-Ura, Hiroto
AU - Jikihara, Shinya
AU - Yamamoto, Takayuki
AU - Endo, Noriyuki
AU - Moriyama, Shunsuke
AU - Nagahisa, Eizoh
AU - Sato, Minoru
PY - 2005/7
Y1 - 2005/7
N2 - The partial amino acid sequence including the N- and C-terminal portions of tauropine dehydrogenase (EC 1.5.1.23) 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.
AB - The partial amino acid sequence including the N- and C-terminal portions of tauropine dehydrogenase (EC 1.5.1.23) 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.
KW - Amino acid sequence
KW - Halichondria japonica
KW - Mu-crystallin
KW - Opine dehydrogenase
KW - Ornithine cyclodeaminase
KW - Sponge
KW - Tauropine dehydrogenase
KW - cDNA
UR - http://www.scopus.com/inward/record.url?scp=20544446094&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=20544446094&partnerID=8YFLogxK
U2 - 10.1016/j.cbpc.2005.04.003
DO - 10.1016/j.cbpc.2005.04.003
M3 - Article
C2 - 15914052
AN - SCOPUS:20544446094
VL - 141
SP - 331
EP - 339
JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
SN - 1096-4959
IS - 3
ER -