Amylolytic glycoside hydrolases

Cellular and Molecular Life Sciences, Apr 2016

Štefan Janeček, Birte Svensson

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Amylolytic glycoside hydrolases

Cell. Mol. Life Sci. Amylolytic glycoside hydrolases Sˇ tefan Janecˇek 0 1 2 3 Birte Svensson 0 1 2 3 0 Department of Biology, Faculty of Natural Sciences, University of SS. Cyril and Methodius in Trnava , Na ́m. J. Herdu 2, 91701 Trnava , Slovakia 1 Laboratory of Protein Evolution, Institute of Molecular Biology, Slovak Academy of Sciences , Du ́bravska ́ cesta 21, 84551 Bratislava , Slovakia 2 & Sˇ tefan Janecˇek 3 Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark , Elektrovej Building 375, 2800 Kongens Lyngby , Denmark When in 1991 Bernard Henrissat created the sequencebased classification of glycoside hydrolases (GH) [1], it was not easy to imagine at that time how huge scope and impact the subsequently established new database of Carbohydrate-Active enZymes, CAZy [2], would have. The aamylase family (family GH13) with 40 sequences bearing 10 different enzyme specificities was already from the beginning a bit exceptional compared to, e.g., the other amylolytic enzyme families of b-amylase and glucoamylase each encompassing just 5 sequences and no other specificities [1]. Currently, a-amylase, as a proper enzyme is present in the main a-amylase family GH13 (forming with families GH70 and GH77 the clan GH-H), in families GH57 and GH119, and eventually in GH126 [3]. In addition to catalytic domains annotated to GH families, noncatalytic domains termed carbohydrate-binding modules Amylolytic enzymes; CAZy database; Starch and glycogen metabolism; Structure and function of enzymes; Protein design and evolution - (CBM) facilitating enzyme binding to different saccharides are also organised in sequence-based families as an integral part of the CAZy classification system [ 2 ]. The actual size of the main a-amylase family GH13 with more than 31,500 members and 30 enzyme specificities is really impressive [ 2 ]. The overall concept of the a-amylase family as it is known and accepted today was, however, based not only on GH classification, but resulted from contribution of an enormous amount of both experimental and theoretical studies. Among these pioneering prediction in silico analyses delivered by Birte Svensson and Ann MacGregor [ 4–9 ] have received special attention. In this regard, also the discovery of neopullulanase by Takashi Kuriki [ 10, 11 ], as a universal enzyme capable to catalyse all four main reactions characteristic for the family, i.e., hydrolysis and formation by transglycosylation of both a-1,4- and a-1,6-glycosidic linkages [ 12 ], deserves to be mentioned. The present multi-author review issue was collected in an effort to illustrate and map the universe of amylolytic hydrolases and additional a-glucan modifying enzymes with emphasis on retaining enzymes as well as other enzymes involved in starch biosynthesis, metabolism and oxidative degradation. The entire collection of eleven review articles starts with the story by the team led by Nicole Koropatkin on the Sus operon that constitutes the starch utilisation system in mammalian gut bacteria from the order Bacteroidetes and encodes eight unique proteins responsible for both binding and degradation of starch at the cell surface. The next two reviews written by the group of Birte Svensson and Eiji Suzuki and his co-author are devoted to structure/function and evolution of debranching and branching enzymes, respectively, from families GH13 and GH57 elucidating their nuances not only with regard to primary and tertiary structures but also within taxonomy. Two further reviews prepared by the groups of Magali Remaud-Simeon and Lubbert Dijkhuizen focus on the family GH70 glucansucrases presenting circularly permuted versions of the characteristic family GH13, the former article in addition pays attention to the biotechnologically important GH13 amylosucrase, while the latter highlights the very recent observation of non-permuted glucansucrases interestingly kept classified in family GH70. In the subsequent review, Stefan Janecek and his co-author offer details on three remarkable evolutionary stories concerning relatedness of plant and archaeal aamylases, animal proteins rBAT and 4F2 and microbial aglucosidases—both from the family GH13 as well as the amylomaltases from borreliae of family GH77. The next article delivered by the team headed by Haruhide Mori and Atsuo Kimura illustrates diverse functions of a-glucosidases from the main a-amylase family GH13 compared to those from the related GH31 family that also includes a1,4-glucan lyases producing anhydrofructose as opposed to the a-glucosidases which release a-glucose. The issue continues with the review written by the group of Joerg Fettke with focus on phosphorylation of glucosyl residues of starch during its metabolism mainly within green algae and land plants, which is mediated by two special enzymes called the glucan, water dikinase and the phosphoglucan, water dikinase containing also starchbinding domains of families CBM20 a (...truncated)


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Štefan Janeček, Birte Svensson. Amylolytic glycoside hydrolases, Cellular and Molecular Life Sciences, 2016, pp. 2601-2602, Volume 73, Issue 14, DOI: 10.1007/s00018-016-2240-z