enzyme kinetics & the Lineweaver-Burk equation
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enzyme kinetics & the Lineweaver-Burk equation
directory of Chem Help ASAP videos: https://www.chemhelpasap.com/youtube/ The V vs. S plot can be modeled through the Michaelis-Menten equation, but this type of rectangular hyperbola is historically difficult to analyze for key enzymatic features - namely Km (the Michaelis constant) and Vmax. The double reciprocal version of Michaelis-Menten ...
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Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to calculate the Vmax and KM of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B.1/Vo Slope = KM/VmaxIntercept = -1/KMIntercept = 1/Vmax 01/[S][S] (??)Vo (µmol/min);with no inhibitorVo (µmol/min);with inhibitor AVo (µmol/min);with inhibitor B310.44.12.1514.56.42.91022.511.34.53033.822.66.89040.533.88.1
Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to calculate the Vmax and KM of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B.1/Vo Slope = KM/VmaxIntercept = -1/KMIntercept = 1/Vmax 01/[S][S] (??)Vo (µmol/min);with no inhibitorVo (µmol/min);with inhibitor AVo (µmol/min);with inhibitor B310.44.12.1514.56.42.91022.511.34.53033.822.66.89040.533.88.1
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discuss the limitations of the lineweaver burk plot and suggest alternative secondary plots and compare and contrast their advantagesdisadvantages in analysis of kinetic data 31653
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Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to calculate the Vmax and KM of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B.1/Vo Slope = KM/VmaxIntercept = -1/KMIntercept = 1/Vmax 01/[S][S] (??)Vo (µmol/min);with no inhibitorVo (µmol/min);with inhibitor AVo (µmol/min);with inhibitor B310.44.12.1514.56.42.91022.511.34.53033.822.66.89040.533.88.1
Use the relationships revealed by a Lineweaver-Burk plot and the tabl…
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