The muscle isozyme of lactate dehydrogenase is inhibited by lactate. Steady state kinetic analysis yielded the following data, with lactate either absent or present at a fixed concentration. (a) Pyruvate is the substrate whose concentration is varied in one plot, NADH in the other. Identify each. Use an arrow and the appro- priate letter (b, c, d, or e) to identify each of the following. (b) Reciprocal of Vmax for the uninhibited enzyme. (c) The line representing data obtained in the presence of lactate acting as a competitive inhibitor with respect to the variable substrate. (d) The line representing data obtained in the presence of lactate acting as a mixed inhibitor with respect to the variable substrate.
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- Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.In working skeletal muscle under anaerobic conditions, glyceraldehyde 3-phosphate is converted to pyruvate (the payoff phase of glycolysis), and the pyruvate is reduced to lactate. Write balanced biochemical equations for all the reactions in this process, with the standard free-energy change for eachreaction. Then write the overall or net equation for the payoff phase of glycolysis (with lactate as the end product), including the net standard free-energy change.Based on the action of thiamine pyrophosphate in catalysis of the pyruvate dehydrogenase reaction, suggest a suitable mechanism for the fourth step in the pyruvate decarboxylase reaction in yeast:
- Arrange the balanced biochemical equations for all the reactions in the catabolism of glucose to two molecules of glyceraldehyde 3-phosphate (the preparatory phase of glycolysis). First step Last step Answer Bank Fructose 1,6-bisphosphate - dihydroxyacetone phosphate + glyceraldehyde 3-phosphate Fructose 6-phosphate + ATP →→→→ fructose 1,6-bisphosphate + ADP Glucose + ATP → glucose 6-phosphate + ADP Dihydroxyacetone phosphate glyceraldehyde 3-phosphate Glucose 6-phosphate →→→→ fructose 6-phosphateGlucosidase I catalyzes hydrolysis of specific glucosidase I is a synthetic trisaccharide, glucose-al-2- glucose-al-3-glucose-a-O(CH₂) #COOCH3. Kinetic measurements oligosaccharides containing glucose. obtained using this trisaccharide as substrate in the deoxynorjirimycin at concentrations of 50 μM (), 100 μM absence (x-x) and presence of the inhibitor 1- A) were used to prepare the (-), and 200 μM (4 Lineweaver-Burk plot below: b) Page 3 12) 7. a) V/V (nmol/hr)-1 1.S 1.0- 0.5 1/Trisaccharide (mM)-! Estimate the values for Vmax and KM for the trisaccharide substrate in the absence of the inhibitor. 0.0 -1.0 0.0 One substrate for 1.0 2.0 Determine whether inhibition by 1-deoxynorjirimycin is competitive, non-competitive or neither.The muscle isozyme of lactate dehydrogenase is inhibited by lactate.Steady-state kinetic analysis yielded the following data, with lactate eitherabsent or present at a fixed concentration. (a) Pyruvate is the substrate whose concentration is varied in one plot, NADH in the other. Identify each. Use an arrow and the appropriate letter (b,c,d,ore) to identify each of the following. (b) Reciprocal of Vmax for the uninhibited enzyme. (c) The line representing data obtained in the presence of lactate acting as a competitive inhibitor with respect to the variable substrate. (d) The line representing data obtained in the presence of lactate acting as a noncompetitive inhibitor with respect to the variable substrate. (e) Reciprocal of KM in the presence of lactate acting as a competitive inhibitor. (f) If KM for NADH is 2 x 10-5 M, then which of the following is the most appropriate NADH concentration to use when determining KM for pyruvate: 10-7 M, 10-6 M, 10-5 M, 10-4 M, or 10-3 M?M
- Write balanced biochemical equations for all the reactions in the catabolism of glucose to two molecules of pyruvate (the preparatory & payoff phase of glycolysis), including the standard free-energy change ΔG for each reaction. Then write the overall or net equation of glycolysis, with the net standard free-energy change when one molecule of glucose is converted into 2 molecules of pyruvate.The muscle isozyme of lactate dehydrogenase is inhibited by lactate. Steady- state kinetic analysis yielded the following data, with lactate either absent or present at a fixed concentration. (a) Pyruvate is the substrate whose concentration is varied in one plot, NADH in the other. Identify each. Use an arrow and the appropriate letter (b, c, d, or e) to identify each of the following. (b) Reciprocal of Vmar for the uninhibited enzyme. (c) The line representing data obtained in the presence of lactate acting as a competitive inhibitor with respect to the variable substrate. (d) The line representing data obtained in the presence of lactate acting as a noncompetitive inhibitor with respect to the variable substrate. (e) Reciprocal of KM in the presence of lactate acting as a competitive inhibitor. (f) If KM for NADH is 2 x 10-5 M, then which of the following is the most appropriate NADH concentration to use when determining KM for руruvate: 10 " M, 10 6 М, 10 М, 10 М, or 10> м?The muscle isozyme of lactate dehydrogenase is inhibited by lactate. Steady-state kinetic analysis yielded the following data, with lactate either absent or present at a fixed concentration. (a) Pyruvate is the substrate whose concentration is varied in one plot,NADH in the other. Identify each. Use an arrow and the appropriate letter(b, c, d, or e) to identify each of the following.(b) Reciprocal of Vmax for the uninhibited enzyme.(c) The line representing data obtained in the presence of lactate acting as a competitive inhibitor with respect to the variable substrate.(d) The line representing data obtained in the presence of lactate acting as a noncompetitive inhibitor with respect to the variable substrate.(e) Reciprocal of KM in the presence of lactate acting as a competitiveinhibitor.(f) If KM for NADH is 2 x 10-5 M, then which of the following is the mostappropriate NADH concentration to use when determining KM for pyruvate: 10-7 M, 10-6 M, 10-5 M, 10-4 M, or 10-3 M?
- Arrange the balanced biochemical equations for all the reactions in the payoff phase of glycolysis and the conversion of pyruvate to lactate.The table below shows the purification of liver lactate dehydrogenase. Purification Table of liver LDH Step Crude Extract Ammonium Sulfate DEAE-Sephadex 5'AMP-Sepharose Volume (mL) 200 100 112 40 LDH activity (Units/mL) (mg/mL) [Protein] 47.0 50.00 90.0 63.00 51.0 1.50 137.0/ 0.4 Calculate the LDH yield for the ammonium sulfate step. Provide answer to one decimal only. Show Transcribed Text this is biochemistry and the topic is protein purification could you pleaae show me the full workings even the workings for the comversionsWrite balanced biochemical equations for all the reactions in the catabolism of glucose to two molecules of glyceraldehyde 3-phosphate (the preparatory phase of glycolysis), including the standard free-energy change for each reaction. Then write the overall or net equation for the preparatory phase of glycolysis, with the net standard free-energy change.