Involvement of the C-terminal tail of Arthrobacter ureafaciens sialidase isoenzyme M in cleavage of the internal sialic acid of ganglioside GM1

Masao Iwamori, Takeo Kaido, Yuriko Iwamori, Yasuhiro Ohta, Kentaro Tsukamoto, Shunji Kozaki

研究成果: Article査読

12 被引用数 (Scopus)

抄録

Arthrobacter ureafaciens sialidase comprises four isoenzymes, L, M1, M2 and S, of which L, M1, and M2, but not S, have the unique ability to cleave GM1 ganglioside, but the hydrolysis of GM3 and colominic acid by S occurs at a higher rate than that by L, M1 and M2. Since the N-terminal amino acid sequences of L, M1, M2 and S were shown to be identical on protein sequencing, they were suggested to have arisen from the same protein through truncation at different C-terminal sites. A DNA segment containing an open reading frame was cloned from a genomic library, and the structural gene was found to comprise 2,970 bp encoding a protein of 990 amino acids including a signal peptide at the N-terminus, a conserved FYRIP-region and four Asp boxes. The molecular weights of the isoenzymes determined by MALDI-TOFMS revealed that L, M1, M2 and S should comprise amino acids 39-773, 39-653, 39-655 and 39-528, respectively. In fact, recombinant enzymes M2 and S prepared in Escherichia coli exhibited identical substrate specificities toward gangliosides as those of the purified enzymes. Consequently, the C-terminal tail of isoenzyme M2 might be involved in the hydrolysis of the internal sialic acid of GM1.

本文言語English
ページ(範囲)327-334
ページ数8
ジャーナルJournal of Biochemistry
138
3
DOI
出版ステータスPublished - 09-2005
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学

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