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Journal articles on the topic 'Glucosylglycerate'

Author: Grafiati
Published: 4 June 2025
Last updated: 1 August 2025

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1

Goude, Renan, St�phanie Renaud, Sylvie Bonnassie, Th�ophile Bernard та Carlos Blanco. "Glutamine, Glutamate, and α-Glucosylglycerate Are the Major Osmotic Solutes Accumulated by Erwinia chrysanthemi Strain 3937". Applied and Environmental Microbiology 70, № 11 (2004): 6535–41. http://dx.doi.org/10.1128/aem.70.11.6535-6541.2004.

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ABSTRACT Erwinia chrysanthemi is a phytopathogenic soil enterobacterium closely related to Escherichia coli. Both species respond to hyperosmotic pressure and to external added osmoprotectants in a similar way. Unexpectedly, the pools of endogenous osmolytes show different compositions. Instead of the commonly accumulated glutamate and trehalose, E. chrysanthemi strain 3937 promotes the accumulation of glutamine and α-glucosylglycerate, which is a new osmolyte for enterobacteria, together with glutamine. The amounts of the three osmolytes increased with medium osmolarity and were reduced when
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2

Cereija, Tatiana Barros, Susana Alarico, Nuno Empadinhas, and Pedro José Barbosa Pereira. "Production, crystallization and structure determination of a mycobacterial glucosylglycerate hydrolase." Acta Crystallographica Section F Structural Biology Communications 73, no. 9 (2017): 536–40. http://dx.doi.org/10.1107/s2053230x17012419.

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Glucosylglycerate hydrolase is highly conserved among rapidly growing mycobacteria and has been found to be involved in recovery from nitrogen starvation by promoting the rapid mobilization of the glucosylglycerate that accumulates under these conditions. Here, the production, crystallization and structure determination of glucosylglycerate hydrolase fromMycobacterium hassiacumusing two-wavelength anomalous diffraction of selenomethionine-substituted crystals are described. The monoclinic (space groupP21) crystals diffracted to ∼2.0 Å resolution at a synchrotron-radiation source and contained
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3

Cereija, Tatiana Barros, Susana Alarico, Eva C. Lourenço, et al. "The structural characterization of a glucosylglycerate hydrolase provides insights into the molecular mechanism of mycobacterial recovery from nitrogen starvation." IUCrJ 6, no. 4 (2019): 572–85. http://dx.doi.org/10.1107/s2052252519005372.

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Bacteria are challenged to adapt to environmental variations in order to survive. Under nutritional stress, several bacteria are able to slow down their metabolism into a nonreplicating state and wait for favourable conditions. It is almost universal that bacteria accumulate carbon stores to survive during this nonreplicating state and to fuel rapid proliferation when the growth-limiting stress disappears. Mycobacteria are exceedingly successful in their ability to become dormant under harsh circumstances and to be able to resume growth when conditions are favourable. Rapidly growing mycobacte
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4

Sawangwan, Thornthan, Christiane Goedl, and Bernd Nidetzky. "Glucosylglycerol and glucosylglycerate as enzyme stabilizers." Biotechnology Journal 5, no. 2 (2009): 187–91. http://dx.doi.org/10.1002/biot.200900197.

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5

Fernandes, Chantal, Nuno Empadinhas, and Milton S. da Costa. "Single-Step Pathway for Synthesis of Glucosylglycerate in Persephonella marina." Journal of Bacteriology 189, no. 11 (2007): 4014–19. http://dx.doi.org/10.1128/jb.00075-07.

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ABSTRACT A single-step pathway for the synthesis of the compatible solute glucosylglycerate (GG) is proposed based on the activity of a recombinant glucosylglycerate synthase (Ggs) from Persephonella marina. The corresponding gene encoded a putative glycosyltransferase that was part of an operon-like structure which also contained the genes for glucosyl-3-phosphoglycerate synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP), the enzymes that lead to the synthesis of GG through the formation of glucosyl-3-phosphoglycerate. The putative glucosyltransferase gene was expressed in Esc
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6

Cánovas, David, Nuno Borges, Carmen Vargas, Antonio Ventosa, Joaquín J. Nieto та Helena Santos. "Role of Nγ-Acetyldiaminobutyrate as an Enzyme Stabilizer and an Intermediate in the Biosynthesis of Hydroxyectoine". Applied and Environmental Microbiology 65, № 9 (1999): 3774–79. http://dx.doi.org/10.1128/aem.65.9.3774-3779.1999.

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ABSTRACT Strain CHR63 is a salt-sensitive mutant of the moderately halophilic wild-type strain Halomonas elongata DSM 3043 that is affected in the ectoine synthase gene (ectC). This strain accumulates large amounts ofNγ-acetyldiaminobutyrate (NADA), the precursor of ectoine (D. Cánovas, C. Vargas, F. Iglesias-Guerra, L. N. Csonka, D. Rhodes, A. Ventosa, and J. J. Nieto, J. Biol. Chem. 272:25794–25801, 1997). Hydroxyectoine, ectoine, and glucosylglycerate were also identified by nuclear magnetic resonance (NMR) as cytoplasmic organic solutes in this mutant. Accumulation of NADA, hydroxyectoine
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7

Behrends, Volker, Kerstin J. Williams, Victoria A. Jenkins, Brian D. Robertson, and Jacob G. Bundy. "Free Glucosylglycerate Is a Novel Marker of Nitrogen Stress inMycobacterium smegmatis." Journal of Proteome Research 11, no. 7 (2012): 3888–96. http://dx.doi.org/10.1021/pr300371b.

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8

Costa, Joana, Nuno Empadinhas, Luís Gonçalves, Pedro Lamosa, Helena Santos, and Milton S. da Costa. "Characterization of the Biosynthetic Pathway of Glucosylglycerate in the Archaeon Methanococcoides burtonii." Journal of Bacteriology 188, no. 3 (2006): 1022–30. http://dx.doi.org/10.1128/jb.188.3.1022-1030.2006.

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ABSTRACT The pathway for the synthesis of the organic solute glucosylglycerate (GG) is proposed based on the activities of the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP) from Methanococcoides burtonii. A mannosyl-3-phosphoglycerate phosphatase gene homologue (mpgP) was found in the genome of M. burtonii (http://www.jgi.doe.gov ), but an mpgS gene coding for mannosyl-3-phosphoglycerate synthase (MpgS) was absent. The gene upstream of the mpgP homologue encoded a putative glucosyltransferase that was expressed in Escherichia coli. T
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9

Fernandes, Chantal, Vitor Mendes, Joana Costa, et al. "Two Alternative Pathways for the Synthesis of the Rare Compatible Solute Mannosylglucosylglycerate in Petrotoga mobilis." Journal of Bacteriology 192, no. 6 (2010): 1624–33. http://dx.doi.org/10.1128/jb.01424-09.

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ABSTRACT The compatible solute mannosylglucosylglycerate (MGG), recently identified in Petrotoga miotherma, also accumulates in Petrotoga mobilis in response to hyperosmotic conditions and supraoptimal growth temperatures. Two functionally connected genes encoding a glucosyl-3-phosphoglycerate synthase (GpgS) and an unknown glycosyltransferase (gene Pmob_1143), which we functionally characterized as a mannosylglucosyl-3-phosphoglycerate synthase and designated MggA, were identified in the genome of Ptg. mobilis. This enzyme used the product of GpgS, glucosyl-3-phosphoglycerate (GPG), as well a
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10

Pospíšil, S., P. Halada, M. Petříček, and P. Sedmera. "Glucosylglycerate is an osmotic solute and an extracellular metabolite produced byStreptomyces caelestis." Folia Microbiologica 52, no. 5 (2007): 451–56. http://dx.doi.org/10.1007/bf02932103.

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11

Klähn, Stephan, Claudia Steglich, Wolfgang R. Hess, and Martin Hagemann. "Glucosylglycerate: a secondary compatible solute common to marine cyanobacteria from nitrogen-poor environments." Environmental Microbiology 12, no. 1 (2010): 83–94. http://dx.doi.org/10.1111/j.1462-2920.2009.02045.x.

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12

Empadinhas, Nuno, and Milton S. da Costa. "To be or not to be a compatible solute: Bioversatility of mannosylglycerate and glucosylglycerate." Systematic and Applied Microbiology 31, no. 3 (2008): 159–68. http://dx.doi.org/10.1016/j.syapm.2008.05.002.

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13

Sato, Shun, Hiroshi Habe, Keiji Sakaki та Dai Kitamoto. "In vitro evaluation of α-d-glucosylglycerate as a protective solute of biological molecules". New Biotechnology 29 (вересень 2012): S63. http://dx.doi.org/10.1016/j.nbt.2012.08.176.

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14

Liu, Juanjuan, Mengfei Ren, Haoran Ma, et al. "One-pot sustainable synthesis of glucosylglycerate from starch and glycerol through artificial in vitro enzymatic cascade." Bioresource Technology 399 (May 2024): 130611. http://dx.doi.org/10.1016/j.biortech.2024.130611.

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15

Nobre, Ana, Nuno Empadinhas, Maria Fernanda Nobre, et al. "The plant Selaginella moellendorffii possesses enzymes for synthesis and hydrolysis of the compatible solutes mannosylglycerate and glucosylglycerate." Planta 237, no. 3 (2012): 891–901. http://dx.doi.org/10.1007/s00425-012-1808-6.

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16

Franceus, Jorick, and Tom Desmet. "Sucrose Phosphorylase and Related Enzymes in Glycoside Hydrolase Family 13: Discovery, Application and Engineering." International Journal of Molecular Sciences 21, no. 7 (2020): 2526. http://dx.doi.org/10.3390/ijms21072526.

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Sucrose phosphorylases are carbohydrate-active enzymes with outstanding potential for the biocatalytic conversion of common table sugar into products with attractive properties. They belong to the glycoside hydrolase family GH13, where they are found in subfamily 18. In bacteria, these enzymes catalyse the phosphorolysis of sucrose to yield α-glucose 1-phosphate and fructose. However, sucrose phosphorylases can also be applied as versatile transglucosylases for the synthesis of valuable glycosides and sugars because their broad promiscuity allows them to transfer the glucosyl group of sucrose
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17

Costa, Joana, Nuno Empadinhas, and Milton S. da Costa. "Glucosylglycerate Biosynthesis in the Deepest Lineage of the Bacteria: Characterization of the Thermophilic Proteins GpgS and GpgP from Persephonella marina." Journal of Bacteriology 189, no. 5 (2006): 1648–54. http://dx.doi.org/10.1128/jb.00841-06.

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ABSTRACT The pathway for the synthesis of glucosylglycerate (GG) in the thermophilic bacterium Persephonella marina is proposed based on the activities of recombinant glucosyl-3-phosphoglycerate (GPG) synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP). The sequences of gpgS and gpgP from the cold-adapted bacterium Methanococcoides burtonii were used to identify the homologues in the genome of P. marina, which were separately cloned and overexpressed as His-tagged proteins in Escherichia coli. The recombinant GpgS protein of P. marina, unlike the homologue from M. burtonii, whic
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18

Franceus, Jorik, and Tom Desmet. "Sucrose Phosphorylase and Related Enzymes in Glycoside Hydrolase Family 13: Discovery, Application and Engineering." International Journal of Molecular Sciences 21, no. 7 (2020): 2526. https://doi.org/10.3390/ijms21072526.

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<strong>Abstract</strong> Sucrose phosphorylases are carbohydrate-active enzymes with outstanding potential for&nbsp;the biocatalytic conversion of common table sugar into products with attractive properties. They&nbsp;belong to the glycoside hydrolase family GH13, where they are found in subfamily 18. In bacteria,&nbsp;these enzymes catalyse the phosphorolysis of sucrose to yield alpha-glucose 1-phosphate and fructose. However, sucrose phosphorylases can also be applied as versatile transglucosylases for the synthesis&nbsp;of valuable glycosides and sugars because their broad promiscuity allo
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19

Sato, Shun, Atsushi Kishimoto, Dai Kitamoto, Yutaka Takahashi, Yukishige Kondo, and Hiroshi Habe. "Synthesis and Characterization of a Novel Glycolipid with Glucosylglycerate as a Hydrophile Showing Protective Effects on Heat-induced Protein Denaturation." Journal of Oleo Science 68, no. 5 (2019): 493–99. http://dx.doi.org/10.5650/jos.ess19044.

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20

Lamosa, Pedro, Marta V. Rodrigues, Luís G. Gonçalves та ін. "Organic solutes in the deepest phylogenetic branches of the Bacteria: identification of α(1–6)glucosyl-α(1–2)glucosylglycerate in Persephonella marina". Extremophiles 17, № 1 (2012): 137–46. http://dx.doi.org/10.1007/s00792-012-0500-x.

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21

Franceus, Jorick, Denise Pinel, and Tom Desmet. "Glucosylglycerate Phosphorylase, an Enzyme with Novel Specificity Involved in Compatible Solute Metabolism." Applied and Environmental Microbiology 83, no. 19 (2017). http://dx.doi.org/10.1128/aem.01434-17.

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ABSTRACT Family GH13_18 of the carbohydrate-active enzyme database consists of retaining glycoside phosphorylases that have attracted interest with their potential for synthesizing valuable α-sugars and glucosides. Sucrose phosphorylase was believed to be the only enzyme with specificity in this subfamily for many years, but recent work revealed an enzyme with a different function and hinted at an even broader diversity that is left to discover. In this study, a putative sucrose phosphorylase from Meiothermus silvanus that resides in a previously unexplored branch of the family's phylogenetic
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22

Allaert, Yentl, Arthur Leyder, Jorick Franceus, and Tom Desmet. "Strategies for the synthesis of the osmolyte glucosylglycerate and its precursor glycerate." Applied Microbiology and Biotechnology 108, no. 1 (2024). http://dx.doi.org/10.1007/s00253-024-13139-w.

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Abstract Glycosidic osmolytes are widespread natural compounds that protect microorganisms and their macromolecules from the deleterious effects of various environmental stresses. Their protective properties have attracted considerable interest for industrial applications, especially as active ingredients in cosmetics and healthcare products. In that regard, the osmolyte glucosylglycerate is somewhat overlooked. Glucosylglycerate is typically accumulated by certain organisms when they are exposed to high salinity and nitrogen starvation, and its potent stabilizing effects have been demonstrate
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23

Nunes-Costa, Daniela, Ana Maranha, Mafalda Costa, Susana Alarico, and Nuno Empadinhas. "Glucosylglycerate metabolism, bioversatility and mycobacterial survival." Glycobiology, December 26, 2016. http://dx.doi.org/10.1093/glycob/cww132.

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24

Bianchini, Giorgio, Martin Hagemann, and Patricia Sánchez-Baracaldo. "Stochastic Character Mapping, Bayesian Model Selection, and Biosynthetic Pathways Shed New Light on the Evolution of Habitat Preference in Cyanobacteria." Systematic Biology, June 27, 2024. http://dx.doi.org/10.1093/sysbio/syae025.

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Abstract Cyanobacteria are the only prokaryotes to have evolved oxygenic photosynthesis paving the way for complex life. Studying the evolution and ecological niche of cyanobacteria and their ancestors is crucial for understanding the intricate dynamics of biosphere evolution. These organisms frequently deal with environmental stressors such as salinity and drought, and they employ compatible solutes as a mechanism to cope with these challenges. Compatible solutes are small molecules that help maintain cellular osmotic balance in high salinity environments, such as marine waters. Their product
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25

Alarico, Susana, Mafalda Costa, Marta S. Sousa, et al. "Mycobacterium hassiacum recovers from nitrogen starvation with up-regulation of a novel glucosylglycerate hydrolase and depletion of the accumulated glucosylglycerate." Scientific Reports 4, no. 1 (2014). http://dx.doi.org/10.1038/srep06766.

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26

Yang, Ting, Ya-Hui Shao, Li-Zhong Guo, Xiang-Lin Meng, Hao Yu, and Wei-Dong Lu. "Role of N,N-Dimethylglycine and Its Catabolism to Sarcosine in Chromohalobacter salexigens DSM 3043." Applied and Environmental Microbiology 86, no. 17 (2020). http://dx.doi.org/10.1128/aem.01186-20.

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ABSTRACT Chromohalobacter salexigens DSM 3043 can grow on N,N-dimethylglycine (DMG) as the sole C, N, and energy source and utilize sarcosine as the sole N source under aerobic conditions. However, little is known about the genes and enzymes involved in the conversion of DMG to sarcosine in this strain. In the present study, gene disruption and complementation assays indicated that the csal_0990, csal_0991, csal_0992, and csal_0993 genes are responsible for DMG degradation to sarcosine. The csal_0990 gene heterologously expressed in Escherichia coli was proven to encode an unusual DMG dehydrog
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27

Zhang, Chao, Qian Chen, Feiyu Fan, et al. "Directed evolution of alditol oxidase for the production of optically pure D-glycerate from glycerol in the engineered Escherichia coli." Journal of Industrial Microbiology and Biotechnology 48, no. 7-8 (2021). http://dx.doi.org/10.1093/jimb/kuab041.

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Abstract D-glycerate is an attractive chemical for a wide variety of pharmaceutical, cosmetic, biodegradable polymers, and other applications. Now several studies have been reported about the synthesis of glycerate by different biotechnological and chemical routes from glycerol or other feedstock. Here, we present the construction of an Escherichia coli engineered strain to produce optically pure D-glycerate by oxidizing glycerol with an evolved variant of alditol oxidase (AldO) from Streptomyces coelicolor. This is achieved by starting from a previously reported variant mAldO and employing th
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28

Besaury, Ludovic, Lucas Martinet, Estelle Mühle, Dominique Clermont, and Caroline Rémond. "Streptomyces silvae sp. nov., isolated from forest soil." International Journal of Systematic and Evolutionary Microbiology 71, no. 12 (2021). http://dx.doi.org/10.1099/ijsem.0.005147.

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A bacterial strain, named For3T, was isolated from forest soil sampled in Champenoux, France. Based on its 16S rRNA gene sequence, the strain was affiliated to the family Streptomycetaceae and, more specifically, to the genus Streptomyces . The strain had 99.93% 16S rRNA gene sequence similarity to its closest relative strains Streptomyces pratensis ATCC 33331T, Streptomyces anulatus ATCC 27416T, Streptomyces setonii NRRL ISP-5322T and Kitasatospora papulosa NRRL B-16504T. The phylogenomic tree using the genome blast distance phylogeny method showed that the closest relative strain was Strepto
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