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昆虫来源的几丁质酶。

Insect-derived chitinases.

机构信息

Department of Biology/Chemistry, University of Osnabrück, 49069, Osnabrück, Germany,

出版信息

Adv Biochem Eng Biotechnol. 2013;136:19-50. doi: 10.1007/10_2013_207.

DOI:10.1007/10_2013_207
PMID:23748348
Abstract

Insect chitinases belong to family 18 of the glycoside hydrolase superfamily (GH18) and comprise endo-splitting enzymes that retain the anomeric β-(1,4) configuration of the cleavage products. However, some of them have lost their catalytic activity but retained the chitin binding activity and/or possess imaginal disc growth factor activity. In all sequenced insect genomes, multiple genes encode chitinases, which are differentially expressed during development and in various insect tissues. Some of them have nonredundant functions and are essential for growth and development. A characteristic property is their multidomain architecture, which comprises varying numbers of catalytic and chitin-binding domains that are connected by glycosylated serine/threonine linker regions. Based on sequence similarities and domain organization, they have been classified into eight different groups. Insect chitinases have gained increasing interest for use in the biological control of parasites, fungi, and insect pests, and some enzymes have properties that make them highly attractive for biotechnological applications.

摘要

昆虫几丁质酶属于糖苷水解酶超家族(GH18)家族 18,包含保留切割产物的非还原性β-(1,4)构型的内切酶。然而,其中一些已经失去了催化活性,但保留了几丁质结合活性和/或具有 imaginal disc 生长因子活性。在所有已测序的昆虫基因组中,多个基因编码几丁质酶,它们在发育过程中和各种昆虫组织中差异表达。其中一些具有非冗余功能,对生长和发育至关重要。其特征性质是它们的多结构域架构,包含数量不同的催化和几丁质结合结构域,这些结构域通过糖基化丝氨酸/苏氨酸连接区连接。根据序列相似性和结构域组织,它们被分为八个不同的组。昆虫几丁质酶因其在寄生虫、真菌和昆虫害虫的生物防治中的应用而受到越来越多的关注,一些酶的特性使它们在生物技术应用中极具吸引力。

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