A biochemist was exploring the properties of Enzyme X . Enzyme X catalyzed the following reaction.
Galactose-3-phosphate <---> Galactose-2-phosphate.
A biochemist was exploring the properties of Enzyme X . Enzyme X catalyzed the following reaction....
monitoring a reaction catalyzed by an NAD-dependent enzyme, a biochemist noticed that the peak of absorbance at 340nm gradually increases. is this reaction procesding towards the formation of NAD+ or NADH? QUESTION 20 Monitoring a reaction catalyzed by an NAD-dependent enzyme, a biochemist notices that the peak of absorbance at 340 nm gradually increases. Is the reaction proceeding towards the formation of NAD+ or NADH?
A biochemist studies the properties of a metabolic enzyme she has just isolated. She obtains kinetic data in the presence and in the absence of two different inhibitors (A and B). The identity of the inhibitors is unknown but we know that one of these is an substrate analog while the other is an alkylating agent. From the plot above determine: a) Km and Vmax of the enzyme b) which inhibitor is the substrate analog? Which is the alkylating agent?...
25. The AG" for the reaction catalyzed by fructokinase is -8.4 kJ/mol at 37°C. What is the equilibrium constant for this reaction? B. U du 626 26 3.8 * 10-2 1.6 x 10-3 The Key cannot be determined if equilibrium concentrations are not given. 26. You discover a mutant yeast strain with a shortened glycolytic pathway resulting from a new enzyme that catalyzes the following reaction: Glyceraldehyde-3-phosphate + H2 + NAD → 3-phosphoglycerate + NADH + H+ Which of the...
3. The equilibrium constant for the reaction catalyzed by UDP-glucose pyrophosphorylase is approximately UTP H Como nykyvylle ??, Pyrophosphate UDP glucose он он phosphate 2P, Phosphere a. Based on the provided equilibrium constant, how would you describe the likelihood of this reaction to progress in the forward or reverse direction? h How does the presence of the enzyme inorganic pyrophosphatase in our cells increase the yield FUDP-glucose beyond that attainable with UDP-glucose pyrophosphorylase alone?
Describe the enzyme carbonic anhydrase by answering the following question: (a) Which reaction is catalyzed by this enzyme? (2 points) (b) Which cofactor is used by this enzyme? (1 point). (c) Which amino acids of the enzyme, and how many of them coordinate the cofactor? (2 points). (d) How does this cofactor help accelerate the reaction? Think about the chemistry (1 point) and the shift of the equilibrium (1 point).
The following data were recorded for the enzyme-catalyzed reaction. Substrate concentration (M) 6.25 x 100 7.50 x 10 1.00 x 10-4 1.00 x 10-3 Reaction velocity (nM/min) 15 56 60 75 (1) Estimate Km and Vmax- (2) What would V be at S=2.5 x 10-5 ?
The concentration of substrate X is low. What happens to the rate of the enzyme- catalyzed reaction if the concentration of X is doubled? 15. What effect does an increase in the enzyme concentration have on the rate of an enzyme-catalyzed reaction? 16.
4. The following data were obtained for an enzyme-catalyzed reaction. Determine whether the enzyme is an allosteric enzyme. (5pts) Submit graph [S] (M X 104) v (umoles/liter/min) 1 1 2 3 4 5 6 7 2 4 7 15 35 55 75 80 83 85 85 8 9 10 11 12
2-In an enzyme-catalyzed reaction, the rate of the reaction depends on which of the following at very low substrate concentrations? Select one: Neither enzyme concentration nor substrate concentration Enzyme concentration but not substrate concentration Substrate concentration but not enzyme concentration Both substrate concentration and enzyme concentration
Pysical Chemistry! Please show all work thank you. 8. A chemist obtains the following Lineweaver-Burk plots for an enzyme catalyzed reaction in the absence and presence of two different inhibitors, A and B. The linear fit for no inhibition is 302.61.96 x 105 .0 x 10 2.5 x 10 2.0 x 10 1.5x 10 1.0 x10 The linear fit for inhibitor A is: 757.82.03 x 105 No inhibitor And the linear fit for inhibitor B is 50 к 10°- 1015.35.95...