Sandbox324: Difference between revisions
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SwissDock and Chimera allowed for protein-ligand docking studies. Many of the highlighted interactions were ester-containing ligands and others were susceptible to hydrolysis. The hydrolase activity of the protein needed to be tested with a substrate known to work with hydrolases. This substrate is p-nitrophenyl acetate PNP when hydrolyzed produces a yellow colored product. The yellow product will lead to the solution absorbing more at 405nm. <ref>Zhang, S.; Sun, W.; Xu, L.; Zheng, X.; Chu, X.; Tian, J.; Wu, N.; Fan, Y. Identification of the Para-Nitrophenol Catabolic Pathway, and Characterization of Three Enzymes Involved in the Hydroquinone Pathway, in Pseudomonas Sp. 1-7. BMC Microbiology 2012, 12 (1). https://doi.org/10.1186/1471-2180-12-27. | SwissDock and Chimera allowed for protein-ligand docking studies. Many of the highlighted interactions were ester-containing ligands and others were susceptible to hydrolysis. The hydrolase activity of the protein needed to be tested with a substrate known to work with hydrolases. This substrate is p-nitrophenyl acetate PNP when hydrolyzed produces a yellow colored product. The yellow product will lead to the solution absorbing more at 405nm. <ref>Zhang, S.; Sun, W.; Xu, L.; Zheng, X.; Chu, X.; Tian, J.; Wu, N.; Fan, Y. Identification of the Para-Nitrophenol Catabolic Pathway, and Characterization of Three Enzymes Involved in the Hydroquinone Pathway, in Pseudomonas Sp. 1-7. BMC Microbiology 2012, 12 (1). https://doi.org/10.1186/1471-2180-12-27. | ||
</ref>. This allows for the activity of the enzyme to be tracked by measuring the increase in absorbance over time. The isolated protein was introduced to p-nitrophenyl acetate in a buffer with a determined optimal pH of 6. Enzyme activity was measured via a change in absorbance at 405nm over 80 minutes. The data collected was consistent with that of hydrolases in other studies.<ref> | </ref>. This allows for the activity of the enzyme to be tracked by measuring the increase in absorbance over time. The isolated protein was introduced to p-nitrophenyl acetate in a buffer with a determined optimal pH of 6. Enzyme activity was measured via a change in absorbance at 405nm over 80 minutes. The data collected was consistent with that of hydrolases in other studies.<ref>Vázquez-Mayorga, E.; Díaz-Sánchez, Á.; Dagda, R.; Domínguez-Solís, C.; Dagda, R.; Coronado-Ramírez, C.; Martínez-Martínez, A. Novel Redox-Dependent Esterase Activity (EC 3.1.1.2) for DJ-1: Implications for Parkinson’s Disease. International Journal of Molecular Sciences 2016, 17 (8), 1346. https://doi.org/10.3390/ijms17081346. | ||
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[[Image:Enzymeactivity.jpeg]] | [[Image:Enzymeactivity.jpeg]] | ||
== Structural highlights == | == Structural highlights == | ||
