PPT - Km Vmax Kcat PowerPoint Presentation, free download - ID:3206146
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PPT - Km Vmax Kcat PowerPoint Presentation, free download - ID:3206146
Km is [S] at 1/2 Vmax It is a constant for a given enzyme at a particular temp and pressure Km is unique to each Enzyme and Substrate. It describes properties of enzyme-substrate interactions. Dependent on temp, pH etc. Independent of enzyme conc .
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Calculate Km and Vmax using both Michaelis-Menten and Lineweaver-Burk equations from the following data:[S], mMVo = mmol/min0.10.340.20.530.40.740.80.911.61.04Determine the type of inhibition of an enzymatic reaction from the following data collected in the presence and absence of the inhibitor:[S], mMVo = mM/minVo with I present (mM/min)11.30.822.01.242.81.783.62.2124.02.4The enzyme fumarase catalyzes the reaction:Fumarate H2O → malateKm is 2.5 x 10^-5 M and Vmax is 225 µmol.min^-1-mg^-1.S
Calculate Km and Vmax using both Michaelis-Menten and Lineweaver-Burk equations from the following data:[S], mMVo = mmol/min0.10.340.20.530.40.740.80.911.61.04Determine the type of inhibition of an enzymatic reaction from the following data collected in the presence and absence of the inhibitor:[S], mMVo = mM/minVo with I present (mM/min)11.30.822.01.242.81.783.62.2124.02.4The enzyme fumarase catalyzes the reaction:Fumarate H2O → malateKm is 2.5 x 10^-5 M and Vmax is 225 µmol.min^-1-mg^-1.S
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Calculate Km and Vmax using both Michaelis-Menten and Lineweaver-Burk equations from the following data:[S], mMVo = mmol/min0.10.340.20.530.40.740.80.911.61.04Determine the type of inhibition of an enzymatic reaction from the following data collected in the presence and absence of the inhibitor:[S], mMVo = mM/minVo with I present (mM/min)11.30.822.01.242.81.783.62.2124.02.4The enzyme fumarase catalyzes the reaction:Fumarate H2O → malateKm is 2.5 x 10^-5 M and Vmax is 225 µmol.min^-1-mg^-1.S
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