FEBS Letters | |
vAL‐1, a novel polysaccharide lyase encoded by chlorovirus CVK2 | |
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
【 预 览 】
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