Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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- The isoelectric point (pI) of 6-phosphogluconate dehydrogenase is 6.0. Explain why the buffer used in DEAE cellulose chromatography must have a pH greater than 6 but less than 9 in order for the enzyme to bind to the DEAE resin.arrow_forwardPropose a full mechanism for the formation of the diene. Show curved arrows to illustrate electron flow, and please show all steps. Include a brief paragraph that describes the steps of the mechanism and discusses the driving force for the steps shown. (attached is the image)arrow_forwardCalculate AG for this reaction under the following conditions: 37°C, pH 7, [Pyruvate] = [CO₂] = 4.0 mM, [OAA] = 2.0 mM, [ATP] = 3.5 mM, [P;] = 5.0 mM, and [ADP] = 1.8 mM. Use 2 signficant figures. AG= i kJ.mol-1 Under these conditions, the reaction is (Tolerance is +/- 2%)arrow_forward
- Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energy change for this reaction at energy change for this reaction at 37.0 ˚C (310 K). AG' for the reaction is +29.7 kJ/mol. Assume that the reaction occurs at pH 7. [malate] = 1.45 mM AG: [oxaloacetate] = 0.130 mM [NAD+ ] = 110 mM [NADH] = 44 mM 47.06 Incorrect kJ.mol-1arrow_forwardHow does one plot the lineweaver burk plot using this data.arrow_forwardDuring glycolysis, glucose is converted into fructose-6- phosphate in two successive reactions: glucose + ATP glucose 6-phosphate + ADP glucose 6-phosphate fructose 6-phosphate The AG' for the overall reaction is: +15.0 kJ/mol. -18.4 kJ/mol. -16.7 kJ/mol. → -15.0 kJ/mol. +18.4 kJ/mol. AG¹⁰ = -16.7 kJ/mol AG¹⁰ = +1.7 kJ/molarrow_forward
- Refer to the figure shown here, and determine the value of E for the overall oxidation/reduction reaction (refer to the book/lecture slides if you need help with the overall reaction). 121/202 + 2H+ + 2e → H₂0 NAD + H* + 2e → NADH O-1.136 volts O 0.496 volts O+1.136 volts voltsm -0.496 volts EU (volts) +0.816 - 0.320arrow_forwardWhich of the reactions are spontaneous (favorable)? C6H130,P + ATP → › C6H14º₁₂P2 + ADP AG = -14.2 kJ/mol L-malate + NAD+ → oxaloacetate + NADH + H+ AG = 29.7 kJ/mol glutamate + NAD+ + H₂O → NH‡ + α-ketoglutarate + NADH + H+ AG = 3.7 kcal/mol → CH2O4 + H2O AG = 3.1 kJ/mol * CąHẠO, — CH,O4 + H,O DHAP C₂H + H₂ glyceraldehyde-3-phosphate AG = 3.8 kJ/mol Rh(I) C2H6 AG-150.97 kJ/molarrow_forwardDetermine whether the following reactions will be spontaneous under standard biochemical conditions. Include calculations for Delta G in your answer. Use Table 13-7 in your textbook to help you.a) 2NADH + 2H+ + O2 --> 2NAD+ + 2H2Ob) Malate + FAD --> Oxaloacetate + FADH2c) Pyruvate + H2S --> Lactate + Sarrow_forward
- Refer to Table to explain why FAD rather than NAD+ is used in the succinate dehydrogenase reaction.arrow_forwardFor the following enzymes (3-6) predict how the conditions will most likely affect the enzymes activity with one of the following and provide a 1 sentence explanation: a. increase activity b. decrease activity c. not likely to alter activity 3) alpha-ketoglutarate dehydrogenase complex binding to AMP when [AMP] is high. 4) phosphohexose isomerase binding NADH when [NADH] is high 5) phosphofructose-1 binding NAD+ when [NAD+] is high 6) pyruvate dehydrogenase complex binding to ATP when [ATP] is higharrow_forwardThe oxidation of Gly-3-P to 1,3-bisphosphoglycerate proceeds with an unfavorable AG which equals 6.3 KJ/mol, yet the flow through this point in the glycolytic pathway proceeds smoothly. Why???arrow_forward
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