Amylolytic glycoside hydrolases

Janeček, Štefan; Svensson, Birte

doi:10.1007/s00018-016-2240-z

Cited by 8 publications

(5 citation statements)

References 12 publications

(14 reference statements)

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“…The content of each GH in F. prausnitzii was similar and low. The function of GHs is to carry out the hydrolysis reaction of glycosides ( Janecek and Svensson, 2016 ).…”

Section: Resultsmentioning

confidence: 99%

Comprehensive analysis of 84 Faecalibacterium prausnitzii strains uncovers their genetic diversity, functional characteristics, and potential risks

Bai

Zhang²,

Jin³

et al. 2023

Front. Cell. Infect. Microbiol.

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Faecalibacterium prausnitzii is a beneficial human gut microbe and a candidate for next-generation probiotics. With probiotics now being used in clinical treatments, concerns about their safety and side effects need to be considered. Therefore, it is essential to obtain a comprehensive understanding of the genetic diversity, functional characteristics, and potential risks of different F. prausnitzii strains. In this study, we collected the genetic information of 84 F . prausnitzii strains to conduct a pan-genome analysis with multiple perspectives. Based on single-copy genes and the sequences of 16S rRNA and the compositions of the pan-genome, different phylogenetic analyses of F. prausnitzii strains were performed, which showed the genetic diversity among them. Among the proteins of the pan-genome, we found that the accessory clusters made a greater contribution to the primary genetic functions of F. prausnitzii strains than the core and specific clusters. The functional annotations of F. prausnitzii showed that only a very small number of proteins were related to human diseases and there were no secondary metabolic gene clusters encoding harmful products. At the same time, complete fatty acid metabolism was detected in F. prausnitzii. In addition, we detected harmful elements, including antibiotic resistance genes, virulence factors, and pathogenic genes, and proposed the probiotic potential risk index (PPRI) and probiotic potential risk score (PPRS) to classify these 84 strains into low-, medium-, and high-risk groups. Finally, 15 strains were identified as low-risk strains and prioritized for clinical application. Undoubtedly, our results provide a comprehensive understanding and insight into F. prausnitzii, and PPRI and PPRS can be applied to evaluate the potential risks of probiotics in general and to guide the application of probiotics in clinical application.

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“…The content of each GH in F. prausnitzii was similar and low. The function of GHs is to carry out the hydrolysis reaction of glycosides ( Janecek and Svensson, 2016 ).…”

Section: Resultsmentioning

confidence: 99%

Comprehensive analysis of 84 Faecalibacterium prausnitzii strains uncovers their genetic diversity, functional characteristics, and potential risks

Bai

Zhang²,

Jin³

et al. 2023

Front. Cell. Infect. Microbiol.

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“…The GH57 family comprises an expanding number of activities since the discovery of α-amylases with unrelated sequences to the GH13 family. , There are a limited number of bacterial and archeal GH57 enzymes with known three dimensional structures associated to the α-glucan metabolism: the 4-α-glucanotransferase (EC 2.4.1.25) and the glycogen branching enzyme (EC 2.4.1.18). , The reported enzymes comprise an N-terminal incomplete TBF, containing a short helix (often called subdomain B) emerging from β2, an intermediate five-helix domain, and a C-terminal β-super sandwich domain . The incomplete TBF has a (β/α) 7 topology including a β-barrel with a distorted toroidal shape.…”

Section: The Catalytic Folds Observed In Prokaryotic α-Glucan Process...mentioning

confidence: 99%

Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes

Cifuente,

Colleoni,

Kalscheuer

et al. 2024

Chem. Rev.

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Bacteria have acquired sophisticated mechanisms for assembling and disassembling polysaccharides of different chemistry. α-D-Glucose homopolysaccharides, so-called α-glucans, are the most widespread polymers in nature being key components of microorganisms. Glycogen functions as an intracellular energy storage while some bacteria also produce extracellular assorted α-glucans. The classical bacterial glycogen metabolic pathway comprises the action of ADP-glucose pyrophosphorylase and glycogen synthase, whereas extracellular α-glucans are mostly related to peripheral enzymes dependent on sucrose. An alternative pathway of glycogen biosynthesis, operating via a maltose 1phosphate polymerizing enzyme, displays an essential wiring with the trehalose metabolism to interconvert disaccharides into polysaccharides. Furthermore, some bacteria show a connection of intracellular glycogen metabolism with the genesis of extracellular capsular α-glucans, revealing a relationship between the storage and structural function of these compounds. Altogether, the current picture shows that bacteria have evolved an intricate α-glucan metabolism that ultimately relies on the evolution of a specific enzymatic machinery. The structural landscape of these enzymes exposes a limited number of core catalytic folds handling many different chemical reactions. In this Review, we present a rationale to explain how the chemical diversity of α-glucans emerged from these systems, highlighting the underlying structural evolution of the enzymes driving α-glucan bacterial metabolism.

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“…In the sequence-based classification of glycoside hydrolases, BspAG13_31A belongs to glycoside hydrolase family 13 (GH13) [ 12 ]. This family is one of the largest GH families and includes a wide variety of amylolytic enzymes such as α-amylase (EC 3.2.1.1), cyclodextrin glucanotransferase (EC 2.4.1.19), branching enzyme (EC 2.4.1.18), and AGase [ 13 , 14 ]. This large GH13 is subdivided into 46 subfamilies based on phylogenetic analysis [ 15 , 16 ], and subfamily 31 (GH13_31) includes AGases and enzymes acting on α-glucosides, such as oligo-1,6-glucosidase (EC 3.2.1.10), dextran glucosidase, and isomaltulose synthase (EC 5.4.99.11).…”

Section: Introductionmentioning

confidence: 99%

Alteration of Substrate Specificity and Transglucosylation Activity of GH13_31 α-Glucosidase from Bacillus sp. AHU2216 through Site-Directed Mutagenesis of Asn258 on β→α Loop 5

et al. 2023

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α-Glucosidase catalyzes the hydrolysis of α-d-glucosides and transglucosylation. Bacillus sp. AHU2216 α-glucosidase (BspAG13_31A), belonging to the glycoside hydrolase family 13 subfamily 31, specifically cleaves α-(1→4)-glucosidic linkages and shows high disaccharide specificity. We showed previously that the maltose moiety of maltotriose (G3) and maltotetraose (G4), covering subsites +1 and +2 of BspAG13_31A, adopts a less stable conformation than the global minimum energy conformation. This unstable d-glucosyl conformation likely arises from steric hindrance by Asn258 on β→α loop 5 of the catalytic (β/α)8-barrel. In this study, Asn258 mutants of BspAG13_31A were enzymatically and structurally analyzed. N258G/P mutations significantly enhanced trisaccharide specificity. The N258P mutation also enhanced the activity toward sucrose and produced erlose from sucrose through transglucosylation. N258G showed a higher specificity to transglucosylation with p-nitrophenyl α-d-glucopyranoside and maltose than the wild type. E256Q/N258G and E258Q/N258P structures in complex with G3 revealed that the maltose moiety of G3 bound at subsites +1 and +2 adopted a relaxed conformation, whereas a less stable conformation was taken in E256Q. This structural difference suggests that stabilizing the G3 conformation enhances trisaccharide specificity. The E256Q/N258G-G3 complex formed an additional hydrogen bond between Met229 and the d-glucose residue of G3 in subsite +2, and this interaction may enhance transglucosylation.

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Amylolytic glycoside hydrolases

Cited by 8 publications

References 12 publications

Comprehensive analysis of 84 Faecalibacterium prausnitzii strains uncovers their genetic diversity, functional characteristics, and potential risks

Comprehensive analysis of 84 Faecalibacterium prausnitzii strains uncovers their genetic diversity, functional characteristics, and potential risks

Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes

Alteration of Substrate Specificity and Transglucosylation Activity of GH13_31 α-Glucosidase from Bacillus sp. AHU2216 through Site-Directed Mutagenesis of Asn258 on β→α Loop 5

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