The Experts below are selected from a list of 200172 Experts worldwide ranked by ideXlab platform
Xu Shen - One of the best experts on this subject based on the ideXlab platform.
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bioChemical characterization and inhibitor discovery of shikimate dehydrogenase from helicobacter pylori
FEBS Journal, 2006Co-Authors: Cong Han, Xu Shen, Hualiang Jiang, Lirui Wang, Lili Chen, Kaixian ChenAbstract:Shikimate dehydrogenase (SDH) is the fourth enzyme involved in the shikimate pathway. It catalyzes the NADPH-dependent reduction of 3-dehydroshikimate to shikimate, and has been developed as a promising target for the discovery of antimicrobial agent. In this report, we identified a new aroE gene encoding SDH from Helicobacter pylori strain SS1. The recombinant H. pylori shikimate dehydrogenase (HpSDH) was cloned, expressed, and purified in Escherichia coli system. The enzymatic characterization of HpSDH demonstrates its activity with kcat of 7.7 s−1 and Km of 0.148 mm toward shikimate, kcat of 7.1 s−1 and Km of 0.182 mm toward NADP, kcat of 5.2 s−1 and Km of 2.9 mm toward NAD. The optimum pH of the enzyme activity is between 8.0 and 9.0, and the optimum temperature is around 60 °C. Using high throughput screening against our Laboratory Chemical library, five compounds, curcumin (1), 3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate (2), butyl 2-{[3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl]oxy}propanoate (3), 2-({2-[(2-{[2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl}-1,3-benzothiazol-6-yl)amino]-2-oxoethyl}sulfanyl)-N-(2-naphthyl)acetamide (4), and maesaquinone diacetate (5) were discovered as HpSDH inhibitors with IC50 values of 15.4, 3.9, 13.4, 2.9, and 3.5 µm, respectively. Further investigation indicates that compounds 1, 2, 3, and 5 demonstrate noncompetitive inhibition pattern, and compound 4 displays competitive inhibition pattern with respect to shikimate. Compounds 1, 4, and 5 display noncompetitive inhibition mode, and compounds 2 and 3 show competitive inhibition mode with respect to NADP. Antibacterial assays demonstrate that compounds 1, 2, and 5 can inhibit the growth of H. pylori with MIC of 16, 16, and 32 µg·mL−1, respectively. This current work is expected to favor better understanding the features of SDH and provide useful information for the development of novel antibiotics to treat H. pylori-associated infection.
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bioChemical characterization and inhibitor discovery of shikimate dehydrogenase from helicobacter pylori
FEBS Journal, 2006Co-Authors: Cong Han, Xu Shen, Hualiang Jiang, Lirui Wang, Lili Chen, Kaixian ChenAbstract:Shikimate dehydrogenase (SDH) is the fourth enzyme involved in the shikimate pathway. It catalyzes the NADPH-dependent reduction of 3-dehydroshikimate to shikimate, and has been developed as a promising target for the discovery of antimicrobial agent. In this report, we identified a new aroE gene encoding SDH from Helicobacter pylori strain SS1. The recombinant H. pylori shikimate dehydrogenase (HpSDH) was cloned, expressed, and purified in Escherichia coli system. The enzymatic characterization of HpSDH demonstrates its activity with k(cat) of 7.7 s(-1) and K(m) of 0.148 mm toward shikimate, k(cat) of 7.1 s(-1) and K(m) of 0.182 mm toward NADP, k(cat) of 5.2 s(-1) and K(m) of 2.9 mm toward NAD. The optimum pH of the enzyme activity is between 8.0 and 9.0, and the optimum temperature is around 60 degrees C. Using high throughput screening against our Laboratory Chemical library, five compounds, curcumin (1), 3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate (2), butyl 2-{[3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl]oxy}propanoate (3), 2-({2-[(2-{[2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl}-1,3-benzothiazol-6-yl)amino]-2-oxoethyl}sulfanyl)-N-(2-naphthyl)acetamide (4), and maesaquinone diacetate (5) were discovered as HpSDH inhibitors with IC(50) values of 15.4, 3.9, 13.4, 2.9, and 3.5 microm, respectively. Further investigation indicates that compounds 1, 2, 3, and 5 demonstrate noncompetitive inhibition pattern, and compound 4 displays competitive inhibition pattern with respect to shikimate. Compounds 1, 4, and 5 display noncompetitive inhibition mode, and compounds 2 and 3 show competitive inhibition mode with respect to NADP. Antibacterial assays demonstrate that compounds 1, 2, and 5 can inhibit the growth of H. pylori with MIC of 16, 16, and 32 microg.mL(-1), respectively. This current work is expected to favor better understanding the features of SDH and provide useful information for the development of novel antibiotics to treat H. pylori-associated infection.
Joshua M Pearce - One of the best experts on this subject based on the ideXlab platform.
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Chemical compatibility of fused filament fabrication-based 3-D printed components with solutions commonly used in semiconductor wet processing
Additive Manufacturing, 2018Co-Authors: Ismo T.s. Heikkinen, Christoffer Kauppinen, Sanja M. Asikainen, Zhengjun Liu, Steven Spoljaric, Jukka V Seppälä, Hele Savin, Joshua M PearceAbstract:3-D printing shows great potential in laboratories for making customized labware and reaction vessels. In addition, affordable fused filament fabrication (FFF)-based 3-D printing has successfully produced high-quality and affordable scientific equipment, focusing on tools without strict Chemical compatibility limitations. As the additives and colorants used in 3-D printing filaments are proprietary, their compatibility with common Chemicals is unknown, which has prevented their widespread use in Laboratory Chemical processing. In this study, the compatibility of ten widely available FFF plastics with solvents, acids, bases and solutions used in the wet processing of semiconductor materials is explored. The results provide data on materials unavailable in the literature and the Chemical properties of 3-D printable plastics that were, are in line with literature. Overall, many 3-D printable plastics are compatible with concentrated solutions. Polypropylene emerged as a promising 3-D printable material for semiconductor processing due to its tolerance of strongly oxidizing acids, such as nitric and sulfuric acids. In addition, 3-D printed custom tools were demonstrated for a range of wet processing applications. The results show that 3-D printed plastics are potential materials for bespoke Chemically resistant labware at less than 10% of the cost of such purchased tools. However, further studies are required to ascertain if such materials are fully compatible with clean room processing.
Hualiang Jiang - One of the best experts on this subject based on the ideXlab platform.
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bioChemical characterization and inhibitor discovery of shikimate dehydrogenase from helicobacter pylori
FEBS Journal, 2006Co-Authors: Cong Han, Xu Shen, Hualiang Jiang, Lirui Wang, Lili Chen, Kaixian ChenAbstract:Shikimate dehydrogenase (SDH) is the fourth enzyme involved in the shikimate pathway. It catalyzes the NADPH-dependent reduction of 3-dehydroshikimate to shikimate, and has been developed as a promising target for the discovery of antimicrobial agent. In this report, we identified a new aroE gene encoding SDH from Helicobacter pylori strain SS1. The recombinant H. pylori shikimate dehydrogenase (HpSDH) was cloned, expressed, and purified in Escherichia coli system. The enzymatic characterization of HpSDH demonstrates its activity with kcat of 7.7 s−1 and Km of 0.148 mm toward shikimate, kcat of 7.1 s−1 and Km of 0.182 mm toward NADP, kcat of 5.2 s−1 and Km of 2.9 mm toward NAD. The optimum pH of the enzyme activity is between 8.0 and 9.0, and the optimum temperature is around 60 °C. Using high throughput screening against our Laboratory Chemical library, five compounds, curcumin (1), 3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate (2), butyl 2-{[3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl]oxy}propanoate (3), 2-({2-[(2-{[2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl}-1,3-benzothiazol-6-yl)amino]-2-oxoethyl}sulfanyl)-N-(2-naphthyl)acetamide (4), and maesaquinone diacetate (5) were discovered as HpSDH inhibitors with IC50 values of 15.4, 3.9, 13.4, 2.9, and 3.5 µm, respectively. Further investigation indicates that compounds 1, 2, 3, and 5 demonstrate noncompetitive inhibition pattern, and compound 4 displays competitive inhibition pattern with respect to shikimate. Compounds 1, 4, and 5 display noncompetitive inhibition mode, and compounds 2 and 3 show competitive inhibition mode with respect to NADP. Antibacterial assays demonstrate that compounds 1, 2, and 5 can inhibit the growth of H. pylori with MIC of 16, 16, and 32 µg·mL−1, respectively. This current work is expected to favor better understanding the features of SDH and provide useful information for the development of novel antibiotics to treat H. pylori-associated infection.
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bioChemical characterization and inhibitor discovery of shikimate dehydrogenase from helicobacter pylori
FEBS Journal, 2006Co-Authors: Cong Han, Xu Shen, Hualiang Jiang, Lirui Wang, Lili Chen, Kaixian ChenAbstract:Shikimate dehydrogenase (SDH) is the fourth enzyme involved in the shikimate pathway. It catalyzes the NADPH-dependent reduction of 3-dehydroshikimate to shikimate, and has been developed as a promising target for the discovery of antimicrobial agent. In this report, we identified a new aroE gene encoding SDH from Helicobacter pylori strain SS1. The recombinant H. pylori shikimate dehydrogenase (HpSDH) was cloned, expressed, and purified in Escherichia coli system. The enzymatic characterization of HpSDH demonstrates its activity with k(cat) of 7.7 s(-1) and K(m) of 0.148 mm toward shikimate, k(cat) of 7.1 s(-1) and K(m) of 0.182 mm toward NADP, k(cat) of 5.2 s(-1) and K(m) of 2.9 mm toward NAD. The optimum pH of the enzyme activity is between 8.0 and 9.0, and the optimum temperature is around 60 degrees C. Using high throughput screening against our Laboratory Chemical library, five compounds, curcumin (1), 3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate (2), butyl 2-{[3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl]oxy}propanoate (3), 2-({2-[(2-{[2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl}-1,3-benzothiazol-6-yl)amino]-2-oxoethyl}sulfanyl)-N-(2-naphthyl)acetamide (4), and maesaquinone diacetate (5) were discovered as HpSDH inhibitors with IC(50) values of 15.4, 3.9, 13.4, 2.9, and 3.5 microm, respectively. Further investigation indicates that compounds 1, 2, 3, and 5 demonstrate noncompetitive inhibition pattern, and compound 4 displays competitive inhibition pattern with respect to shikimate. Compounds 1, 4, and 5 display noncompetitive inhibition mode, and compounds 2 and 3 show competitive inhibition mode with respect to NADP. Antibacterial assays demonstrate that compounds 1, 2, and 5 can inhibit the growth of H. pylori with MIC of 16, 16, and 32 microg.mL(-1), respectively. This current work is expected to favor better understanding the features of SDH and provide useful information for the development of novel antibiotics to treat H. pylori-associated infection.
Ismo T.s. Heikkinen - One of the best experts on this subject based on the ideXlab platform.
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Chemical compatibility of fused filament fabrication-based 3-D printed components with solutions commonly used in semiconductor wet processing
Additive Manufacturing, 2018Co-Authors: Ismo T.s. Heikkinen, Christoffer Kauppinen, Sanja M. Asikainen, Zhengjun Liu, Steven Spoljaric, Jukka V Seppälä, Hele Savin, Joshua M PearceAbstract:3-D printing shows great potential in laboratories for making customized labware and reaction vessels. In addition, affordable fused filament fabrication (FFF)-based 3-D printing has successfully produced high-quality and affordable scientific equipment, focusing on tools without strict Chemical compatibility limitations. As the additives and colorants used in 3-D printing filaments are proprietary, their compatibility with common Chemicals is unknown, which has prevented their widespread use in Laboratory Chemical processing. In this study, the compatibility of ten widely available FFF plastics with solvents, acids, bases and solutions used in the wet processing of semiconductor materials is explored. The results provide data on materials unavailable in the literature and the Chemical properties of 3-D printable plastics that were, are in line with literature. Overall, many 3-D printable plastics are compatible with concentrated solutions. Polypropylene emerged as a promising 3-D printable material for semiconductor processing due to its tolerance of strongly oxidizing acids, such as nitric and sulfuric acids. In addition, 3-D printed custom tools were demonstrated for a range of wet processing applications. The results show that 3-D printed plastics are potential materials for bespoke Chemically resistant labware at less than 10% of the cost of such purchased tools. However, further studies are required to ascertain if such materials are fully compatible with clean room processing.
Cong Han - One of the best experts on this subject based on the ideXlab platform.
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bioChemical characterization and inhibitor discovery of shikimate dehydrogenase from helicobacter pylori
FEBS Journal, 2006Co-Authors: Cong Han, Xu Shen, Hualiang Jiang, Lirui Wang, Lili Chen, Kaixian ChenAbstract:Shikimate dehydrogenase (SDH) is the fourth enzyme involved in the shikimate pathway. It catalyzes the NADPH-dependent reduction of 3-dehydroshikimate to shikimate, and has been developed as a promising target for the discovery of antimicrobial agent. In this report, we identified a new aroE gene encoding SDH from Helicobacter pylori strain SS1. The recombinant H. pylori shikimate dehydrogenase (HpSDH) was cloned, expressed, and purified in Escherichia coli system. The enzymatic characterization of HpSDH demonstrates its activity with kcat of 7.7 s−1 and Km of 0.148 mm toward shikimate, kcat of 7.1 s−1 and Km of 0.182 mm toward NADP, kcat of 5.2 s−1 and Km of 2.9 mm toward NAD. The optimum pH of the enzyme activity is between 8.0 and 9.0, and the optimum temperature is around 60 °C. Using high throughput screening against our Laboratory Chemical library, five compounds, curcumin (1), 3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate (2), butyl 2-{[3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl]oxy}propanoate (3), 2-({2-[(2-{[2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl}-1,3-benzothiazol-6-yl)amino]-2-oxoethyl}sulfanyl)-N-(2-naphthyl)acetamide (4), and maesaquinone diacetate (5) were discovered as HpSDH inhibitors with IC50 values of 15.4, 3.9, 13.4, 2.9, and 3.5 µm, respectively. Further investigation indicates that compounds 1, 2, 3, and 5 demonstrate noncompetitive inhibition pattern, and compound 4 displays competitive inhibition pattern with respect to shikimate. Compounds 1, 4, and 5 display noncompetitive inhibition mode, and compounds 2 and 3 show competitive inhibition mode with respect to NADP. Antibacterial assays demonstrate that compounds 1, 2, and 5 can inhibit the growth of H. pylori with MIC of 16, 16, and 32 µg·mL−1, respectively. This current work is expected to favor better understanding the features of SDH and provide useful information for the development of novel antibiotics to treat H. pylori-associated infection.
-
bioChemical characterization and inhibitor discovery of shikimate dehydrogenase from helicobacter pylori
FEBS Journal, 2006Co-Authors: Cong Han, Xu Shen, Hualiang Jiang, Lirui Wang, Lili Chen, Kaixian ChenAbstract:Shikimate dehydrogenase (SDH) is the fourth enzyme involved in the shikimate pathway. It catalyzes the NADPH-dependent reduction of 3-dehydroshikimate to shikimate, and has been developed as a promising target for the discovery of antimicrobial agent. In this report, we identified a new aroE gene encoding SDH from Helicobacter pylori strain SS1. The recombinant H. pylori shikimate dehydrogenase (HpSDH) was cloned, expressed, and purified in Escherichia coli system. The enzymatic characterization of HpSDH demonstrates its activity with k(cat) of 7.7 s(-1) and K(m) of 0.148 mm toward shikimate, k(cat) of 7.1 s(-1) and K(m) of 0.182 mm toward NADP, k(cat) of 5.2 s(-1) and K(m) of 2.9 mm toward NAD. The optimum pH of the enzyme activity is between 8.0 and 9.0, and the optimum temperature is around 60 degrees C. Using high throughput screening against our Laboratory Chemical library, five compounds, curcumin (1), 3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate (2), butyl 2-{[3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl]oxy}propanoate (3), 2-({2-[(2-{[2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl}-1,3-benzothiazol-6-yl)amino]-2-oxoethyl}sulfanyl)-N-(2-naphthyl)acetamide (4), and maesaquinone diacetate (5) were discovered as HpSDH inhibitors with IC(50) values of 15.4, 3.9, 13.4, 2.9, and 3.5 microm, respectively. Further investigation indicates that compounds 1, 2, 3, and 5 demonstrate noncompetitive inhibition pattern, and compound 4 displays competitive inhibition pattern with respect to shikimate. Compounds 1, 4, and 5 display noncompetitive inhibition mode, and compounds 2 and 3 show competitive inhibition mode with respect to NADP. Antibacterial assays demonstrate that compounds 1, 2, and 5 can inhibit the growth of H. pylori with MIC of 16, 16, and 32 microg.mL(-1), respectively. This current work is expected to favor better understanding the features of SDH and provide useful information for the development of novel antibiotics to treat H. pylori-associated infection.
