Structure of a glycoside hydrolase family 50 enzyme from a subfamily that is enriched in human gut microbiome bacteroidetes

Giles, Kaleigh; Pluvinage, B.; Boraston, A.B.

doi:10.1002/prot.25189

Cited by 12 publications

(9 citation statements)

References 16 publications

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“…Second, we attempted to determine the activity of Bp GH50, which possibly takes part in the next step of the agarose degradation pathway by degrading neoagarooligosaccharides (NAOSs; agarooligosaccharides with AHG on the non-reducing end) into NeoDP2. As previously reported 33 , Bp GH50 did not exhibit an exo-type β-agarase activity producing NeoDP2 toward agarose (Fig. 2 C).…”

Section: Resultssupporting

confidence: 87%

Metabolic and enzymatic elucidation of cooperative degradation of red seaweed agarose by two human gut bacteria

Yun

Park

et al. 2021

Sci Rep

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Various health beneficial outcomes associated with red seaweeds, especially their polysaccharides, have been claimed, but the molecular pathway of how red seaweed polysaccharides are degraded and utilized by cooperative actions of human gut bacteria has not been elucidated. Here, we investigated the enzymatic and metabolic cooperation between two human gut symbionts, Bacteroides plebeius and Bifidobacterium longum ssp. infantis, with regard to the degradation of agarose, the main carbohydrate of red seaweed. More specifically, B. plebeius initially decomposed agarose into agarotriose by the actions of the enzymes belonging to glycoside hydrolase (GH) families 16 and 117 (i.e., BpGH16A and BpGH117) located in the polysaccharide utilization locus, a specific gene cluster for red seaweed carbohydrates. Then, B. infantis extracted energy from agarotriose by the actions of two agarolytic β-galactosidases (i.e., Bga42A and Bga2A) and produced neoagarobiose. B. plebeius ultimately acted on neoagarobiose by BpGH117, resulting in the production of 3,6-anhydro-l-galactose, a monomeric sugar possessing anti-inflammatory activity. Our discovery of the cooperative actions of the two human gut symbionts on agarose degradation and the identification of the related enzyme genes and metabolic intermediates generated during the metabolic processes provide a molecular basis for agarose degradation by gut bacteria.

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Section: Resultssupporting

confidence: 87%

Metabolic and enzymatic elucidation of cooperative degradation of red seaweed agarose by two human gut bacteria

Yun

Park

et al. 2021

Sci Rep

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“…Three crystal structures of GH50 agarases have also been determined—exo‐β‐agarase (Aga50D) from Saccharophagus degradans (PDB ID: 4BQ2), β‐agarase from Bacteroides plebeius (PDB ID: 5T3B), and an exo‐β‐agarase from A. gilvus WH0801 (PDB ID: 5Z6P). These enzymes display a core (α/β) 8 ‐barrel fold and the key Glu residues are well conserved (Figure 8D, 8E, and 8F) (Giles, Pluvinage, & Boraston, 2016; Pluvinage, Hehemann, & Boraston, 2013; Zhang et al., 2019). Enzyme kinetics and degradation pattern data obtained with various oligosaccharides of agarose with AgaB from Pseudoalteromonas sp.…”

Section: Marine‐polysaccharide Degrading Enzymesmentioning

confidence: 99%

Marine‐polysaccharide degrading enzymes: Status and prospects

Sun

Gao

Xue

et al. 2020

Comp Rev Food Sci Food Safe

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Marine-polysaccharide degrading enzymes have recently been studied extensively. They are particularly interesting as they catalyze the cleavage of glycosidic bonds in polysaccharide macromolecules and produce oligosaccharides with low degrees of polymerization. Numerous findings have demonstrated that marine polysaccharides and their biotransformed products possess beneficial properties including antitumor, antiviral, anticoagulant, and anti-inflammatory activities, and they have great value in healthcare, cosmetics, the food industry, and agriculture. Exploitation of enzymes that can degrade marine polysaccharides is in the ascendant, and is important for high-value use of marine biomass resources. In this review, we describe research and prospects regarding the classification, biochemical properties, and catalytic mechanisms of the main types of marine-polysaccharide degrading enzymes, focusing on chitinase, chitosanase, alginate lyase, agarase, and carrageenase, and their product oligosaccharides. The state-of-the-art discussion of marine-polysaccharide degrading enzymes and their properties offers information that might enable more efficient production of marine oligosaccharides. We also highlight current problems in the field of marine-polysaccharide degrading enzymes and trends in their development. Understanding the properties, catalytic mechanisms, and modification of known enzymes will aid the identification of novel enzymes to degrade marine polysaccharides and facilitation of their use in various biotechnological processes. K E Y W O R D S agarase, alginate lyase, carrageenase, chitinase, chitosanase 1 INTRODUCTION Ocean occupies >70% of the global surface, and the vast oceanic water environment has spawned large and complex marine ecosystems with rich biodiversity. There is a wide variety of marine resources, however, they are largely unexploited. This situation makes the marine environment very attractive for bioprospecting to discover new functions and molecules (Arnaud-Haond, Arrieta, & Duarte, 2011). Research into marine compounds, especially polysaccharides from renewable biomass, is attracting increasing attention. Polysaccharides make up one of the largest

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“…Previous studies have shown that heat stress can alter the gut microbiota of mice [ 17 ]. The Firmicutes to Bacteroidetes ratio decreased significantly under 30 °C [ 18 ]. Short-chain fatty acids (SCFAs) are metabolites formed by gut microbes from complex dietary carbohydrates.…”

Section: Introductionmentioning

confidence: 99%

Effects of Heat Stress on Gut-Microbial Metabolites, Gastrointestinal Peptides, Glycolipid Metabolism, and Performance of Broilers

Wang

Zhou

et al. 2021

Animals

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This paper investigated the effects of heat stress on gut-microbial metabolites, gastrointestinal peptides, glycolipid metabolism, and performance of broilers. Thus, 132 male Arbor Acres broilers, 28-days-old, were randomly distributed to undergo two treatments: thermoneutral control (TC, 21 °C) and high temperature (HT, 31 °C). The results showed that the average daily gain (ADG), average daily feed intake (ADFI), and gastric inhibitory polypeptide (GIP) concentration in the jejunum significantly decreased the core temperature, feed conversion ratio (FCR), and ghrelin of the hypothalamus, and cholecystokinin (CCK) in jejunum, and serum significantly increased in the HT group (p < 0.05). Exploration of the structure of cecal microbes was accomplished by sequencing 16S rRNA genes. The sequencing results showed that the proportion of Christensenellaceae and Lachnospiraceae decreased significantly whereas the proportion of Peptococcaceae increased at the family level (p < 0.05). Ruminococcus and Clostridium abundances significantly increased at the genus level. Furthermore, the content of acetate in the HT group significantly increased. Biochemical parameters showed that the blood glucose concentration of the HT group significantly decreased, and the TG (serum triglycerides), TC (total cholesterol), insulin concentration, and the insulin resistance index significantly increased. Nonesterified fatty acid (NEFA) in the HT group decreased significantly. In conclusion, the results of this paper suggest that the poor production performance of broilers under heat stress may be related to short-chain fatty acids (SCFAs) fermented by intestinal microbiota involved in regulating metabolic disorders.

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Structure of a glycoside hydrolase family 50 enzyme from a subfamily that is enriched in human gut microbiome bacteroidetes

Cited by 12 publications

References 16 publications

Metabolic and enzymatic elucidation of cooperative degradation of red seaweed agarose by two human gut bacteria

Metabolic and enzymatic elucidation of cooperative degradation of red seaweed agarose by two human gut bacteria

Marine‐polysaccharide degrading enzymes: Status and prospects

Effects of Heat Stress on Gut-Microbial Metabolites, Gastrointestinal Peptides, Glycolipid Metabolism, and Performance of Broilers

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