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PMID: 14960306 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

vAL-1, a novel polysaccharide lyase encoded by chlorovirus CVK2.

FEBS letters ·Vol. 559 ·No. 1-3 ·2004-02-13 ·Pages 51-6

Sugimoto I, Onimatsu H, Fujie M, Usami S, Yamada T

Abstract

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 beta- or alpha-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.

MeSH Terms
Cell Wall/chemistry,metabolism Chlorella/virology Kinetics Oligosaccharides/analysis,chemistry Polysaccharide-Lyases/classification,metabolism Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Uronic Acids/analysis
Chemicals
Oligosaccharides Uronic Acids Polysaccharide-Lyases vAL-1 protein, chlorovirus CVK2
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Sugimoto Ichiro
Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima 739-8530, Japan.
Onimatsu Hideki
Fujie Makoto
Usami Shoji
Yamada Takashi
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2004-02-13
Pages
51-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
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