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Diverse and common features of trehalases and their contributions to microbial trehalose metabolism.
Applied Microbiology and Biotechnology ( IF 5 ) Pub Date : 2020-01-10 , DOI: 10.1007/s00253-019-10339-7
Masayoshi Sakaguchi 1
Affiliation  

Trehalose is a stable disaccharide that consists of two glucose units linked primarily by an α,α-(1 → 1)-linkage, and it has been found in a wide variety of organisms. In these organisms, trehalose functions not only as a source of carbon energy but also as a protector against various stress conditions. In addition, this disaccharide is attractive for use in a wide range of applications due to its bioactivities. In trehalose metabolism, direct trehalose-hydrolyzing enzymes are known as trehalases, which have been reported for bacteria, archaea, and eukaryotes, and are classified into glycoside hydrolase 37 (GH37), GH65, and GH15 families according to the Carbohydrate-Active enZyme (CAZy) database. The catalytic domains (CDs) of these enzymes commonly share (α/α)6-barrel structures and have two amino acid residues, Asp and/or Glu, that function as catalytic residues in an inverting mechanism. In this review, I focus on diverse and common features of trehalases within different GH families and their contributions to microbial trehalose metabolism.

中文翻译:

海藻糖酶的多样性和共同特征及其对微生物海藻糖代谢的贡献。

海藻糖是一种稳定的二糖,由两个主要通过α,α-(1→1)链接的葡萄糖单元组成,并且已在多种生物中发现。在这些生物中,海藻糖不仅充当碳能量的来源,而且还充当抵御各种压力条件的保护剂。此外,由于其生物活性,该二糖具有广泛的应用前景。在海藻糖代谢中,直接海藻糖水解酶称为海藻糖酶,据报道可用于细菌,古细菌和真核生物,根据碳水化合物活性酶分类为糖苷水解酶37(GH37),GH65和GH15家族( CAZy)数据库。这些酶的催化结构域(CD)通常共享(α/α)6-桶状结构,并具有两个氨基酸残基,即Asp和/或Glu,在转化机理中起催化残基的作用。在这篇综述中,我重点介绍了不同GH家族中海藻糖酶的多样性和共同特征,以及它们对微生物海藻糖代谢的贡献。
更新日期:2020-01-11
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