Crystal Structure of Amylomaltase from <i>Corynebacterium glutamicum</i>

Joo, Seongjoon; Kim, Sang Woo; Seo, Hogyun; Kim, Kyungjin

doi:10.1021/acs.jafc.6b02296

Cited by 14 publications

(42 citation statements)

References 48 publications

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“…Our results may contradict previous reports on the diet of these birds indicating their capacity to select plants (or parts of plants) with high-nutritional value (low in fiber) in all periods [1,8]. However, the high presence of GH families encompassing genes for the degradation of starch (e.g.GH77, with amylomaltase activity [59]) (Table 3), and genes involved in starch metabolism (e.g. starch phosphorylase [EC.2.4.1.1]) also indicates that starch-containing compounds may constitute an important part of the nutrition in the wild ptarmigan diet.…”

Section: Discussioncontrasting

confidence: 96%

Characterization of the cecum microbiome from wild and captive rock ptarmigans indigenous to Arctic Norway

et al. 2019

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Rock ptarmigans (Lagopus muta) are gallinaceous birds inhabiting arctic and sub-arctic environments. Their diet varies by season, including plants or plant parts of high nutritional value, but also toxic plant secondary metabolites (PSMs). Little is known about the microbes driving organic matter decomposition in the cecum of ptarmigans, especially the last steps leading to methanogenesis. The cecum microbiome in wild rock ptarmigans from Arctic Norway was characterized to unveil their functional potential for PSM detoxification, methanogenesis and polysaccharides degradation. Cecal samples were collected from wild ptarmigans from Svalbard (L. m. hyperborea) and northern Norway (L. m. muta) during autumn/winter (Sept-Dec). Samples from captive Svalbard ptarmigans fed commercial pelleted feed were included to investigate the effect of diet on microbial composition and function. Abundances of methanogens and bacteria were determined by qRT-PCR, while microbial community composition and functional potential were studied using 16S rRNA gene sequencing and shotgun metagenomics. Abundances of bacteria and methanogenic Archaea were higher in wild ptarmigans compared to captive birds. The ceca of wild ptarmigans housed bacterial groups involved in PSM-degradation, and genes mediating the conversion of phenol compounds to pyruvate. Methanomassiliicoccaceae was the major archaeal family in wild ptarmigans, carrying the genes for methanogenesis from methanol. It might be related to increased methanol production from pectin degradation in wild birds due to a diet consisting of primarily fresh pectin-rich plants. Both wild and captive ptarmigans possessed a broad suite of genes for the depolymerization of hemicellulose and non-cellulosic polysaccharides (e.g. starch). In conclusion, there were no physiological and phenotypical dissimilarities in the microbiota found in the cecum of wild ptarmigans on mainland Norway and Svalbard. While substantial differences in the functional potential for PSM degradation and methanogenesis in wild and captive birds seem to be a direct consequence of their dissimilar diets.

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Section: Discussioncontrasting

confidence: 96%

Characterization of the cecum microbiome from wild and captive rock ptarmigans indigenous to Arctic Norway

et al. 2019

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“…In comparison with CGTase that mainly produces small ring cyclodextrins (SR-CDs) with 6-8 mer, AM showed fewer number of domains [49,50]. EcAM [51] and CgAM [52] share only 30% identity of protein sequences but both of them similarly represent an additional N-terminal domain, so-called domain N (Figure 1B). The subdomains N1 and N2 are linked by a short linker of nine amino acid residues.…”

Section: Overall Structure Of Amylomaltasementioning

confidence: 99%

Production of Large-Ring Cyclodextrins by Amylomaltases

et al. 2022

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Amylomaltase is a well-known glucan transferase that can produce large ring cyclodextrins (LR-CDs) or so-called cycloamyloses via cyclization reaction. Amylomaltases have been found in several microorganisms and their optimum temperatures are generally around 60–70 °C for thermostable amylomaltases and 30–45 °C for the enzymes from mesophilic bacteria and plants. The optimum pHs for mesophilic amylomaltases are around pH 6.0–7.0, while the thermostable amylomaltases are generally active at more acidic conditions. Size of LR-CDs depends on the source of amylomaltases and the reaction conditions including pH, temperature, incubation time, and substrate. For example, in the case of amylomaltase from Corynebacterium glutamicum, LR-CD productions at alkaline pH or at a long incubation time favored products with a low degree of polymerization. In this review, we explore the synthesis of LR-CDs by amylomaltases, structural information of amylomaltases, as well as current applications of LR-CDs and amylomaltases.

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“…They are characterized by the presence of a N -domain of about 160 amino acids in front of the TIM-barrel catalytic domain. Phyre2 analysis showed that the A. cellulolyticus sequence can be folded in a 3D model with 100% confidence with the structure of the amylomaltase from the bacterium C. glutamicum [ 7 ]. The percentage of identity of the two sequences is about 42%.…”

Section: Structural Analysesmentioning

confidence: 99%

“…The percentage of identity of the two sequences is about 42%. A possible role of the N -terminal domain could be that of a carbohydrate-binding module (CBM) as the presence of an immunoglobulin-like β-sandwich fold would suggest [ 7 ]. Currently, the A. cellulolyticus enzyme is the only extreme amylomaltase possessing the N -terminal domain to have been expressed as a recombinant protein and functionally tested.…”

Section: Structural Analysesmentioning

confidence: 99%

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Amylomaltases in Extremophilic Microorganisms

et al. 2021

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Amylomaltases (4-α-glucanotransferases, E.C. 2.4.1.25) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of α-1,4′-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4′-position of an α-1,4′-d-glucan acceptor. The intramolecular reaction produces a cyclic α-1,4′-glucan. Amylomaltases can be found only in prokaryotes, where they are involved in glycogen degradation and maltose metabolism. These enzymes are being studied for possible biotechnological applications, such as the production of (i) sugar substitutes; (ii) cycloamyloses (molecules larger than cyclodextrins), which could potentially be useful as carriers and encapsulating agents for hydrophobic molecules and also as effective protein chaperons; and (iii) thermoreversible starch gels, which could be used as non-animal gelatin substitutes. Extremophilic prokaryotes have been investigated for the identification of amylomaltases to be used in the starch modifying processes, which require high temperatures or extreme conditions. The aim of this article is to present an updated overview of studies on amylomaltases from extremophilic Bacteria and Archaea, including data about their distribution, activity, potential industrial application and structure.

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Crystal Structure of Amylomaltase from Corynebacterium glutamicum

Cited by 14 publications

References 48 publications

Characterization of the cecum microbiome from wild and captive rock ptarmigans indigenous to Arctic Norway

Characterization of the cecum microbiome from wild and captive rock ptarmigans indigenous to Arctic Norway

Production of Large-Ring Cyclodextrins by Amylomaltases

Amylomaltases in Extremophilic Microorganisms

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