does the amount of enzyme affecy the kinetic data?
does the amount of enzyme affecy the kinetic data?
Homework Answers
Yes; increasing enzyme concentration will speed up the reaction, as long as there is substrate available to bind to it.
The kinetic data given below are for an enzyme in the absence and presence of a...
The kinetic data given below are for an enzyme in the absence and presence of a reversible inhibitor. From the data, generate both a Michaelis-Menten and Linweaver-Burk Plot for both that uninbibited and inhibited reactions. Graph both the uninhibited and inhibited data on the same plot. From these data calculate the Vmax and Km for the enzyme in absence and presence of the inhibitor. Is the inhibitor working cometitively or noncompetitively? Explain. [S], mM Vo, mM/min Vo, mM, min with...
- Vmax is a kinetic property associated with an enzyme. Describe what occurs when an enzyme...
- Vmax is a kinetic property associated with an enzyme. Describe what occurs when an enzyme reaches its Vmax. - Km is also another intrinsic property of an enzyme. Practically, what does the Km tell about how an enzyme interacts with its substrate?
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the following conditions: in the absence of an inhibitor, and in the presence of two different inhibitors, (1) and (2) each at a concentration of 10 mM. Assume the total enzyme concentration, [Elo, is the same for all reactions and the enzyme obeys the Michaelis-Menten mechanism In the presence of presence of 10 mM inhibitor 1 inhibitor2 In the 10 mM No inhibitor mM 2.5...
1 Graphic depictions of enzyme kinetic data can and in evaluation of reversible enzyme inhibition. Please...
1 Graphic depictions of enzyme kinetic data can and in evaluation of reversible enzyme inhibition. Please use the data below to determine type of inhibition for using two different concentrations (in blue and purple). Be sure to include graphical representation (Michaelis-Menton. I Lineweaver-Burk plots), type of inhibition, appropriate kinetic schemes and rate equations. The enzyme concentration at its initial state E, was kept constant. All data points are given in arbitrary units. Completely justify your answer. Use Excel or graphing...
1. Graphic depictions of enzyme kinetic data can aid in evaluation of reversible enzyme inhibition. Please...
1. Graphic depictions of enzyme kinetic data can aid in evaluation of reversible enzyme inhibition. Please use the data below to determine type of inhibition for using two different concentrations (in blue and purple). Be sure to include graphical representation (Michaelis-Menton, Lineweaver-Burk plots), type of inhibition, appropriate kinetic schemes and rate equations. The enzyme concentration at its initial state E, was kept constant. All data points are given in arbitrary units. Completely justify your answer. Use Excel or graphing paper...
1. The following kinetic data was generated for the Hst enzyme. The overall reaction for this...
1. The following kinetic data was generated for the Hst enzyme. The overall reaction for this enzyme is: OH ОН + NH3 NH2 All reactions are carried out in a final reaction volume of 2 mL with 0.1ug of purified Hst protein present at pH 7.8. The Hst protein has a molecular weight of 90 kDa based on estimates from gel filtration column chromatography and a molecular weight of 45 kDa based on estimates from denaturing SDS PAGE gel electrophoresis....
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of an inhibitor at 5 mM concentration (2). Assume[ET] is the same in each experiment. [S] (MM) (1) v(umol/mL sec) 12 (2) v(umol/mL sec) 4.3 1 8 2 4 20 29 14 21 8 35 12 40 26 a. Using a graphing program (excel or sigmaplot) construct a lineweaver burke plot representing the uninhibited reaction and the inhibited...
included proper units when HLLL 1. The following kinetic data were generated for the enzyme SpB1,...
included proper units when HLLL 1. The following kinetic data were generated for the enzyme SpB1, this enzyme has an unknown biological function. Using the information provided below answer questions la-le. All reactions had 0.1 mg/mL SPBT which based on amino acid sequence and gel filtration column chromatography has a molecular weight of 42,500 Daltons. S002- Substrate 1 Substrate 2 KM (MM) kcat (sec) glucose >50 <0.01 glucose NADP 4+1 0.5+0.07 glucose NAD 2718 2 +0.05 galactose >50 <0.01 galactose...
The following observations come from Lineweaver-Burke plots, based on kinetic data generated from a Michaelis/Menton-type enzyme...
The following observations come from Lineweaver-Burke plots, based on kinetic data generated from a Michaelis/Menton-type enzyme (E) that catalyzes the hydrolysis of a peptide substrate (S). All data were generated in the presence of 18.0 μM total enzyme. The enzyme-catalyzed reaction has a Km of 3.00 μM and a Vmax of 2.00 μM/sec. The enzyme-catalyzed reaction in the presence of 15.0 μM of Inhibitor A has an apparent Km of 2.25 μM and an apparent Vmax of 1.50 μM/sec. The...
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a...
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a series of assays where you measured the rate of reactions as you varied the concentration of substrate in each assay (Table A). Estimate from a Michaelis-Menten plot approximate values for Vmax, KM, Kcat, and the specificity constant for this enzyme and substrate. (The only information that is given is this paragraph and the table below). Table 1: [S] (μM) v (μmol/L/min) 0 0 5...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the following conditions: in the absence of an inhibitor, and in the presence of two different inhibitors, (1) and (2) each at a concentration of 10 mM. Assume the total enzyme concentration, [Elo, is the same for all reactions and the enzyme obeys the Michaelis-Menten mechanism In the presence of presence of 10 mM inhibitor 1 inhibitor2 In the 10 mM No inhibitor mM 2.5...
1 Graphic depictions of enzyme kinetic data can and in evaluation of reversible enzyme inhibition. Please use the data below to determine type of inhibition for using two different concentrations (in blue and purple). Be sure to include graphical representation (Michaelis-Menton. I Lineweaver-Burk plots), type of inhibition, appropriate kinetic schemes and rate equations. The enzyme concentration at its initial state E, was kept constant. All data points are given in arbitrary units. Completely justify your answer. Use Excel or graphing...
1. Graphic depictions of enzyme kinetic data can aid in evaluation of reversible enzyme inhibition. Please use the data below to determine type of inhibition for using two different concentrations (in blue and purple). Be sure to include graphical representation (Michaelis-Menton, Lineweaver-Burk plots), type of inhibition, appropriate kinetic schemes and rate equations. The enzyme concentration at its initial state E, was kept constant. All data points are given in arbitrary units. Completely justify your answer. Use Excel or graphing paper...
1. The following kinetic data was generated for the Hst enzyme. The overall reaction for this enzyme is: OH ОН + NH3 NH2 All reactions are carried out in a final reaction volume of 2 mL with 0.1ug of purified Hst protein present at pH 7.8. The Hst protein has a molecular weight of 90 kDa based on estimates from gel filtration column chromatography and a molecular weight of 45 kDa based on estimates from denaturing SDS PAGE gel electrophoresis....
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of an inhibitor at 5 mM concentration (2). Assume[ET] is the same in each experiment. [S] (MM) (1) v(umol/mL sec) 12 (2) v(umol/mL sec) 4.3 1 8 2 4 20 29 14 21 8 35 12 40 26 a. Using a graphing program (excel or sigmaplot) construct a lineweaver burke plot representing the uninhibited reaction and the inhibited...
included proper units when HLLL 1. The following kinetic data were generated for the enzyme SpB1, this enzyme has an unknown biological function. Using the information provided below answer questions la-le. All reactions had 0.1 mg/mL SPBT which based on amino acid sequence and gel filtration column chromatography has a molecular weight of 42,500 Daltons. S002- Substrate 1 Substrate 2 KM (MM) kcat (sec) glucose >50 <0.01 glucose NADP 4+1 0.5+0.07 glucose NAD 2718 2 +0.05 galactose >50 <0.01 galactose...
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