Glucokinase is a liver enzyme with a kcat of 33/second and a Km for Glucose of...
Glucokinase is a liver enzyme with a kcat of 33/second and a Km
for Glucose of 7 mM. What is the initial reaction rate (in mM
product / second) of 0.1 mM glucokinase in the presence of 50 mM
glucose?
Please show your work clearly.
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Glucokinase is a liver enzyme with a kcat of 33/second and a Km
for Glucose of...
54. What is the catalyze reaction rate? Km=2 mM Kcat= 3 s-1 At the enzyme concentration=10...
54. What is the catalyze reaction rate? Km=2 mM Kcat= 3 s-1 At the enzyme concentration=10 nM and substrate concentration= 3 mM
2 (10 marks)The KM and kcat of a carboxypeptidase isoform were found to be 2.00mM and...
2 (10 marks)The KM and kcat of a carboxypeptidase isoform were found to be 2.00mM and 150s-1 respectively for substrate A. What is the initial rate of the reaction if [A] = 4.00mM and [E]total = 0.010 mM? The presence of a competitive inhibitor [I] = 5.00mM decreases the initial rate by a factor of 2, what is KI?
Values for an Enzyme and a substrate are: Km=4 uM and kcat=20/min. For an experiment where...
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CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. T...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
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Part A An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 uM and a kcat value of 201 s-1. At an initial enzyme concentration of 0.0100 uM, the initial reaction velocity was found to be 1.07 x 10- uM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures. ► View Available Hint(s) PO ALO O O ? [S]; = MM UM
Given the enzyme system just described (Km = 8.20*10-5M and kcat = 40.0 s-1, [Eltot =...
Given the enzyme system just described (Km = 8.20*10-5M and kcat = 40.0 s-1, [Eltot = 2.00*10-7 M), suppose we introduce a classical noncompetitive inhibitor with K1 = 1.20*10-7M. If the concentration of inhibitor introduced is 3.0 um, what will the effective kcat be? Express your answer in s-1.
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...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A B. For substrate...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A B. For substrate A, she determined 30 min that Km 3.0 HM and kcat Jessica graduated and her project has been passed on to you. Unfortunately, Jessica was so busy that she sometimes forgot to record all of the details of an assay in her lab notebook. Your mentor suggests that you try to back calculate some of the missing concentration values. Assume that the enzyme follows...
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Question 2: You have just discovered a new enzyme that catalyzes the degradation of cellulose to glucose. You hope to commercialize this enzyme ultimately to invent a process for biofuel manufacture. In order to determine how efficient the enzyme is and how fast the enzyme catalyzes the reaction, you have to perform some basic enzyme kinetics. Plot the following enzyme data for the enzyme catalyzed reaction and determine the Km and Vmax. Show your graph with correct units on the...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
Part A An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 uM and a kcat value of 201 s-1. At an initial enzyme concentration of 0.0100 uM, the initial reaction velocity was found to be 1.07 x 10- uM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures. ► View Available Hint(s) PO ALO O O ? [S]; = MM UM
Given the enzyme system just described (Km = 8.20*10-5M and kcat = 40.0 s-1, [Eltot = 2.00*10-7 M), suppose we introduce a classical noncompetitive inhibitor with K1 = 1.20*10-7M. If the concentration of inhibitor introduced is 3.0 um, what will the effective kcat be? Express your answer in s-1.
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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