Question

In: Biology

Draw a Michaelis Menten graph to represent normal pyruvate carboxylase kinetics in the conversion of pyruvate...

Draw a Michaelis Menten graph to represent normal pyruvate carboxylase kinetics in the conversion of pyruvate to oxaloacetate. Explain why you drew things as you did.

Solutions

Expert Solution

Michael is menten equation describes the relationship between the concentration of substrate and velocity of an enzyme catalysed reaction. The graph which I have drawn shows pyruvate as the substrate and enzyme is pyruvate carboxylase. It shows that as the concentration of pyruvate increases the rate of reaction also increases. The rate of reaction is highest at a point which we call as maximum velocity. After achieving maximum velocity, the reaction achieves a plateau. It is because now the number of enzyme molecules, that is, the molecules of pyruvate carboxylase has become limited or the number of substrate molecules, pyruvate molecules have become Limited. All the enzyme active sites are occupied by pyruvate molecules. For the increase in the rate of reaction will be seen only if the concentration of enzyme and substrate is increased.

Please rate high.


Related Solutions

In Michaelis-Menten kinetics, what values would make an enzyme “good” at catalysis?
In Michaelis-Menten kinetics, what values would make an enzyme “good” at catalysis?
The conversion of pyruvate into acetyl CoA uses what enzyme? Pyruvate Hydrolase Pyruvate Carboxylase Lactate Dehydrogenase...
The conversion of pyruvate into acetyl CoA uses what enzyme? Pyruvate Hydrolase Pyruvate Carboxylase Lactate Dehydrogenase Citrate Synthase None of the above Jenny’s lungs have an intrapulmonic pressure of 762 mmHg and an intrapleural pressure of 757 mmHg. Atmospheric pressure is 759 mmHg. What is happening to Jenny? Jenny is inhaling Jenny’s ventilation is at a rest Jenny is exhaling Jenny is suffocating None of the above Which of the following enzymes does ubiquinone transport electrons to in the ETC?
What are the key differences between the Michaelis-Menten model that describes enzyme kinetics and the Monod...
What are the key differences between the Michaelis-Menten model that describes enzyme kinetics and the Monod model that describes whole-cell or community kinetics?
Explain the meaning of the three assumptions for the Michaelis-Menten kinetics. Express each assumption in mathematical...
Explain the meaning of the three assumptions for the Michaelis-Menten kinetics. Express each assumption in mathematical terms.
Initial rate data for an enzyme that obeys Michaelis-Menten kinetics are shown in the following table....
Initial rate data for an enzyme that obeys Michaelis-Menten kinetics are shown in the following table. When the enzyme concentration is 3 nmol ml−1, a Lineweaver-Burk plot of this data gives a line with a y-intercept of 0.00426 (μmol−1ml s). [S] μM v0 (μmol ml−1 s−1) 320 169 160 132 80.0 92.0 40.0 57.2 20.0 32.6 10.0 17.5 a. Calculate Kcat for the reaction b. Calculate Km for the enzyme cWhen the reactions in part (B) are repeated in the...
For enzymes that follow Michaelis–Menten kinetics, the inhibitors that inhibit enzyme activity include reversible inhibitor and...
For enzymes that follow Michaelis–Menten kinetics, the inhibitors that inhibit enzyme activity include reversible inhibitor and irreversible inhibitor. 1. Describe the type of reversible inhibitor. 2. Suggest ways to distinguish between types of inhibitors through enzyme reaction experiments.
1.The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics:...
1.The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: 2/27/ 20 V0 (mol/min) 217 325 433 488 647 Substrate added (mmol/L) 0.8 2 4 6 1,000        The Km for A) 1 mM., B) 1000mM, C) 2mM, D ) 4mM, E) 6mM this enzyme is approximately: 2. To A) the enzyme concentration. B) the initial velocity of the catalyzed reaction at [S] >> Km. C) the initial velocity of the catalyzed reaction at...
biochem: Derive the Michaelis–Menten kinetics and note the important assumptions. Also indicate why a double reciprocal...
biochem: Derive the Michaelis–Menten kinetics and note the important assumptions. Also indicate why a double reciprocal plot is linear.
IN MICHAELIS MENTEN GRAPH, HOW WOULD YOU INCREASE VELOCITY BEYOND Vmax?
IN MICHAELIS MENTEN GRAPH, HOW WOULD YOU INCREASE VELOCITY BEYOND Vmax?
Lactate dehydrogenase catalyzes the conversion of pyruvate into lactate. kinetics experiment was done to test the...
Lactate dehydrogenase catalyzes the conversion of pyruvate into lactate. kinetics experiment was done to test the effect of the inhibitor oxamate on the ability of lactate dehydrogenase to convert pyruvate into lactate. The data with and without inhibitor was plotted as a Lineweaver-Burk plot. The velocity is in units of umol/min and the concentration of pyruvate is in units of MM The equation of the line of best fit for the reaction without oxamate is: y 3.1x +7.4 The equation...
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT