vAL‐1, a novel polysaccharide lyase encoded by chlorovirus CVK2

FEBS Letters

Sugimoto, Ichiro¹  Fujie, Makoto¹  Yamada, Takashi¹  Onimatsu, Hideki¹  Usami, Shoji¹ 

[1] Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima 739-8530, Japan

关键词: Chlorella cell wall;    Chlorovirus;    Polysaccharide lyase;    Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry;    vAL-1;    ABEE;    4-aminobenzoic acid ethyl ester;    CWM;    cell wall material;    GST;    glutathione S-transferase;    HPLC;    high-performance liquid chromatography;    MALDI-TOF;    matrix-assisted laser desorption/ionization time-of-flight;    ORF;    open reading frame;    PA;    pyridylamino;    PSD;    post-source decay;    TLC;    thin-layer chromatography;   

DOI  :  10.1016/S0014-5793(04)00022-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cell wall materials isolated from Chlorella cells were degraded by the polysaccharide-degrading enzyme vAL-1 encoded by chlorovirus CVK2. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analyses of the degradation products (oligosaccharides) revealed major oligosaccharides contain unsaturated GlcA at the reducing terminus, and a side chain attached at C2 or C3 of GlcA(C4=C5), which mainly consisted of Ara, GlcNAc and Gal. The results indicated that vAL-1 is a novel polysaccharide lyase, cleaving chains of β- or α-1,4-linked GlcAs. The unique structures of Chlorella cell wall were also revealed. Studies on the complicated structures of naturally occurring polysaccharides will be greatly facilitated by using vAL-1 as a tool in structural analysis.

【 授权许可】

Unknown