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Diverse and common features of trehalases and their contributions to microbial trehalose metabolism.
Appl Microbiol Biotechnol. 2020 Mar; 104(5):1837-1847.AM

Abstract

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.

Authors+Show Affiliations

Department of Chemistry and Life Science, Kogakuin University, 2,665-1 Nakano-cho, Hachioji, Tokyo, 192-0015, Japan. bt11532@ns.kogakuin.ac.jp.

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

31925485

Citation

Sakaguchi, Masayoshi. "Diverse and Common Features of Trehalases and Their Contributions to Microbial Trehalose Metabolism." Applied Microbiology and Biotechnology, vol. 104, no. 5, 2020, pp. 1837-1847.
Sakaguchi M. Diverse and common features of trehalases and their contributions to microbial trehalose metabolism. Appl Microbiol Biotechnol. 2020;104(5):1837-1847.
Sakaguchi, M. (2020). Diverse and common features of trehalases and their contributions to microbial trehalose metabolism. Applied Microbiology and Biotechnology, 104(5), 1837-1847. https://doi.org/10.1007/s00253-019-10339-7
Sakaguchi M. Diverse and Common Features of Trehalases and Their Contributions to Microbial Trehalose Metabolism. Appl Microbiol Biotechnol. 2020;104(5):1837-1847. PubMed PMID: 31925485.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Diverse and common features of trehalases and their contributions to microbial trehalose metabolism. A1 - Sakaguchi,Masayoshi, Y1 - 2020/01/10/ PY - 2019/10/03/received PY - 2019/12/27/accepted PY - 2019/12/13/revised PY - 2020/1/12/pubmed PY - 2020/1/12/medline PY - 2020/1/12/entrez KW - GH15 KW - GH37 KW - GH65 KW - Glycoside hydrolase (GH) family KW - Trehalase KW - Trehalose metabolism SP - 1837 EP - 1847 JF - Applied microbiology and biotechnology JO - Appl. Microbiol. Biotechnol. VL - 104 IS - 5 N2 - 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. SN - 1432-0614 UR - https://www.unboundmedicine.com/medline/citation/31925485/Diverse_and_common_features_of_trehalases_and_their_contributions_to_microbial_trehalose_metabolism_ L2 - https://dx.doi.org/10.1007/s00253-019-10339-7 DB - PRIME DP - Unbound Medicine ER -
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