The Experts below are selected from a list of 360 Experts worldwide ranked by ideXlab platform
Zhigang Qian - One of the best experts on this subject based on the ideXlab platform.
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a novel synthetic pathway for Glutarate production in recombinant escherichia coli
Process Biochemistry, 2017Co-Authors: Xiaoxia Xia, Jianjiang Zhong, Zhigang QianAbstract:Abstract Glutarate is an important C5 linear chain dicarboxylic acid having wide applications in chemical industry. In this work we report Glutarate production by Escherichia coli with a newly constructed biosynthetic pathway containing part of known glutaconate biosynthetic pathway and a gap-filling module employing trans -enoyl-CoA reductase (Ter). Overall the artificial pathway comprises reduction of the central carbon metabolite α-ketoGlutarate to 2-hydroxyGlutarate, activation to 2-hydroxyglutaryl-CoA, dehydration to trans -glutaconyl-CoA, hydrogenation to glutaryl-CoA by Ter and thioester hydrolysis to finally yield Glutarate. The pathway introduced into E. coli resulted in a recombinant strain that produced 3.8 mg/L of Glutarate together with 27.7 mg/L of glutaconate in anaerobic culture mode. The Glutarate production increased by approximately 50% through the mutation of Ter from Treponema denticola . The results demonstrated biosynthesis of Glutarate via a non-natural synthetic pathway, which may enable its biobased production from renewable resources.
Jorg S Hartig - One of the best experts on this subject based on the ideXlab platform.
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widespread bacterial lysine degradation proceeding via Glutarate and l 2 hydroxyGlutarate
Nature Communications, 2018Co-Authors: Sebastian Knorr, Malte Sinn, Dmitry Galetskiy, Rhys M Williams, Changhao Wang, Nicolai Muller, Olga Mayans, David Schleheck, Jorg S HartigAbstract:Lysine degradation has remained elusive in many organisms including Escherichia coli. Here we report catabolism of lysine to succinate in E. coli involving Glutarate and L-2-hydroxyGlutarate as intermediates. We show that CsiD acts as an α-ketoGlutarate-dependent dioxygenase catalysing hydroxylation of Glutarate to L-2-hydroxyGlutarate. CsiD is found widespread in bacteria. We present crystal structures of CsiD in complex with Glutarate, succinate, and the inhibitor N-oxalyl-glycine, demonstrating strong discrimination between the structurally related ligands. We show that L-2-hydroxyGlutarate is converted to α-ketoGlutarate by LhgO acting as a membrane-bound, ubiquinone-linked dehydrogenase. Lysine enters the pathway via 5-aminovalerate by the promiscuous enzymes GabT and GabD. We demonstrate that repression of the pathway by CsiR is relieved upon Glutarate binding. In conclusion, lysine degradation provides an important link in central metabolism. Our results imply the gut microbiome as a potential source of Glutarate and L-2-hydroxyGlutarate associated with human diseases such as cancer and organic acidurias. Lysine degradation and the role of the metabolites Glutarate and L-2-hydroxyGlutarate have remained elusive in many organisms including Escherichia coli. Here authors present a pathway for catabolism of lysine to succinate in E. coli involving Glutarate and L-2-hydroxyGlutarate as intermediates.
Jianjiang Zhong - One of the best experts on this subject based on the ideXlab platform.
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a novel synthetic pathway for Glutarate production in recombinant escherichia coli
Process Biochemistry, 2017Co-Authors: Xiaoxia Xia, Jianjiang Zhong, Zhigang QianAbstract:Abstract Glutarate is an important C5 linear chain dicarboxylic acid having wide applications in chemical industry. In this work we report Glutarate production by Escherichia coli with a newly constructed biosynthetic pathway containing part of known glutaconate biosynthetic pathway and a gap-filling module employing trans -enoyl-CoA reductase (Ter). Overall the artificial pathway comprises reduction of the central carbon metabolite α-ketoGlutarate to 2-hydroxyGlutarate, activation to 2-hydroxyglutaryl-CoA, dehydration to trans -glutaconyl-CoA, hydrogenation to glutaryl-CoA by Ter and thioester hydrolysis to finally yield Glutarate. The pathway introduced into E. coli resulted in a recombinant strain that produced 3.8 mg/L of Glutarate together with 27.7 mg/L of glutaconate in anaerobic culture mode. The Glutarate production increased by approximately 50% through the mutation of Ter from Treponema denticola . The results demonstrated biosynthesis of Glutarate via a non-natural synthetic pathway, which may enable its biobased production from renewable resources.
Tae Wha Moon - One of the best experts on this subject based on the ideXlab platform.
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resistant Glutarate starch from adlay preparation and properties
Carbohydrate Polymers, 2008Co-Authors: Mi Jung Kim, Seung Jun Choi, Sang Ick Shin, Ma Ri Sohn, Chang Joo Lee, Yang Kim, Wan Il Cho, Tae Wha MoonAbstract:Reaction conditions were optimized to increase the content of resistant starch in adlay starch using esterification with glutaric acid, and the physicochemical properties of the prepared Glutarate starches were investigated. Different amounts of glutaric acid (0.1-0.5 g/g starch, dry weight basis) were reacted with adlay starch at various temperatures (70-130 °C) and reaction times (3-9 h). The resistant starch levels increased with increased glutaric acid content, reaction temperature, and reaction time. The color difference was mainly affected by reaction time. The highest resistant starch content (RS 66%) was obtained using conditions of 0.4 g glutaric acid/g starch, 115 °C, and 7.5 h, with a color difference of 10.24. After digestion with α-amylase and amyloglucosidase, the water-soluble fraction of Glutarate starch had more oligosaccharides than high-amylose maize starch (RS 43%). FT-IR and solid-state NMR detected carbonyl groups in the Glutarate starch, indicating the formation of cross-linkages through esterification. The granular structure of the Glutarate starches was not destroyed and they retained birefringence. After heating with an excess of water, the granules kept their shape but lost their birefringence. The Glutarate starches had low solubility in both cold and hot water, and the resistant starch contents were unchanged after heating due to the restriction of swelling by cross-linking. The Glutarate starches had a similar chain-length distribution to raw starch, indicating that acid hydrolysis took place at branching points in the amorphous region. Furthermore, the Glutarate starches possessed a weaker crystalline region, more diverse double helical chains, and lower enthalpy than raw starch.
Debajyoti Ghoshal - One of the best experts on this subject based on the ideXlab platform.
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three dimensional robust porous coordination polymer with schiff base site on the pore wall synthesis single crystal to single crystal reversibility and selective co2 adsorption
Crystal Growth & Design, 2011Co-Authors: Rajdip Dey, Ritesh Haldar, Tapas Kumar Maji, Debajyoti GhoshalAbstract:A three-dimensional (3D) robust porous coordination polymer, {[Cu(azpy)(glut)](H2O)2}n (1) (azpy = N,N′-bis-pyridin-4-ylmethylene-hydrazine, glut = Glutarate), has been synthesized and structurally characterized. Single crystal X-ray diffraction analysis reveals that each of paddle-wheel Cu2(CO2)4 units is connected with Glutarates in the crystallographic bc plane to form a two-dimensional (2D) sheet which is pillared by an azpy linker to afford a 3D porous framework. Controlled heating of the as-synthesized crystal 1 at ∼150 °C under reduced pressure causes a color change of {[Cu(azpy)(glut)]}n (1a) from deep green to light green. The structure determination of the dehydrated compound shows the same framework structure as that of {[Cu(azpy)(glut)](H2O)2}n (1) with the only difference of the nonexistence of lattice water molecules resulting in a large void in the framework. The dehydrated light green crystal 1a regenerates the virgin as-synthesized crystal 1 with the formula of {[Cu(azpy)(glut)](H2O)2}n u...