Carbohydrate esterase family 4 enzymes: substrate specificity

被引:99
作者
Caufrier, F
Martinou, A
Dupont, C
Bouriotis, V
机构
[1] Inst Mol Biol & Biotechnol, Enzyme Biotechnol Div, Iraklion 71110, Crete, Greece
[2] Free Univ Brussels, Vakgrp Microbiol, B-1070 Brussels, Belgium
[3] Univ Crete, Dept Biol, Dept Appl Biol & Biotechnol, Iraklion 71409, Crete, Greece
[4] Univ Quebec, Inst Armand Frappier, INRS, Ctr Microbiol & Biotechnol, Laval, PQ H7V 1B7, Canada
关键词
chitin deacetylase; chitin; acetyl xylan esterase; xylan; peptidoglycan;
D O I
10.1016/S0008-6215(03)00002-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The substrate specificity of selected enzymes classified under Carbohydrate Esterase family 4 (CE4) has been examined. Chitin deacetylase from Mucor rouxii and both a native and a truncated form of acetyl xylan esterase from Streptomyces lividans were found to be active on both xylan and several soluble chitinous substrates. Furthermore, the activities of all enzymes examined were significantly increased in the presence of Co2+ when chitinous substrates were employed. However, the presence of this metal ion did not result in enhancing the activities of the enzymes when xylan was used as substrate. An acetyl xylan esterase from Bacillus pumilus, classified under Carbohydrate Esterase family 7, was found to be inactive towards all chitinous substrates tested. Finally, all enzymes examined were inactive towards cell wall peptidoglycan. (C) 2003 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:687 / 692
页数:6
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