Organic Chemistry
9th Edition
ISBN: 9781305080485
Author: John E. McMurry
Publisher: Cengage Learning
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Chapter 29.SE, Problem 40AP
Interpretation Introduction
a) Transmission
Interpretation:
Transamination is catalyzed by enzyme called transaminases.
Interpretation Introduction
b) Carboxylation of a
Interpretation:
The one important cofactor is Biotin vitamin and the enzyme in pyruvate carboxylase.
Interpretation Introduction
c) Decarboxylation of an α-keto acid
Interpretation:
The enzyme complex catalyzes the oxidative decarboxylation of branched short chain alpha keto acids.
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Chapter 29 Solutions
Organic Chemistry
Ch. 29.1 - Prob. 1PCh. 29.3 - Write the equations for the remaining passages of...Ch. 29.3 - Prob. 3PCh. 29.4 - Write a mechanism for the dehydration reaction of...Ch. 29.4 - Evidence for the role of acetate in fatty-acid...Ch. 29.4 - Does the reduction of acetoacetyl ACP in step 6...Ch. 29.5 - Prob. 7PCh. 29.5 - Look at the entire glycolysis pathway, and make a...Ch. 29.6 - Prob. 9PCh. 29.7 - Prob. 10P
Ch. 29.7 - Write mechanisms for step 2 of the citric acid...Ch. 29.7 - Prob. 12PCh. 29.8 - Prob. 13PCh. 29.9 - Write all the steps in the transamination reaction...Ch. 29.9 - What -keto acid is formed on transamination of...Ch. 29.9 - Prob. 16PCh. 29.SE - Prob. 17VCCh. 29.SE - Identify the following intermediate in the citric...Ch. 29.SE - The following compound is an intermediate in the...Ch. 29.SE - Prob. 20VCCh. 29.SE - In the pentose phosphate pathway for degrading...Ch. 29.SE - Prob. 22MPCh. 29.SE - One of the steps in the pentose phosphate pathway...Ch. 29.SE - One of the steps in the pentose phosphate pathway...Ch. 29.SE - Prob. 25MPCh. 29.SE - Prob. 26MPCh. 29.SE - Prob. 27MPCh. 29.SE - Prob. 28MPCh. 29.SE - Prob. 29MPCh. 29.SE - Prob. 30MPCh. 29.SE - Prob. 31MPCh. 29.SE - Prob. 32APCh. 29.SE - Prob. 33APCh. 29.SE - Prob. 34APCh. 29.SE - Prob. 35APCh. 29.SE - Prob. 36APCh. 29.SE - Prob. 37APCh. 29.SE - Prob. 38APCh. 29.SE - Prob. 39APCh. 29.SE - Prob. 40APCh. 29.SE - Prob. 41APCh. 29.SE - Prob. 42APCh. 29.SE - Prob. 43APCh. 29.SE - Prob. 44APCh. 29.SE - Prob. 45APCh. 29.SE - Prob. 46APCh. 29.SE - Prob. 47APCh. 29.SE - Prob. 48APCh. 29.SE - Prob. 49APCh. 29.SE - Prob. 50APCh. 29.SE - In glycerol metabolism, the oxidation of...Ch. 29.SE - Prob. 52APCh. 29.SE - Prob. 53APCh. 29.SE - Prob. 54APCh. 29.SE - In step 7 of fatty-acid biosynthesis (Figure...Ch. 29.SE - Prob. 56AP
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- What type of reaction would a PLP-containing enzyme catalyze if the bond most perpendicular to PLP was a C-COO- bond? A、racemization B、transamination C、aldol cleavage D、decarboxylationarrow_forwardSuggest a name for an enzyme that catalyzes each of the following reactions. a. Hydrolysis of lactose b. Oxidation of nitrite c. Decarboxylation of citrate d. Reduction of oxalatearrow_forwardWhat type of specificity (absolute, group, linkage, or stereochemical) is associated with each of the following enzymes? a. Sucrase b. A lipase c. A decarboxylase d. L-glutamate oxidasearrow_forward
- What type of specificity (absolute, group, linkage, or stereochemical) is associated with each of the following enzymes? a. A deaminase b. A phosphatase c. Maltase d. L-Lactate dehydrogenasearrow_forwardThe aconitase-catalyzed addition of water to cis-aconitate in the citric acid cycle occurs with the following stereochemistry. Does the addition of the OH group occur on the Re or Si face of the substrate? What about the addition of the H? Do the H and OH groups add from the same side of the double bond or from opposite sides?arrow_forwardIn glycerol metabolism, the oxidation of sn-glycerol 3-phosphate to give dihydroxyacetone phosphate is catalyzed by sn-glycerol-3-phosphate dehydrogenase, with NAD+ as cofactor. The reaction is stereospecific, occurring exclusively on the Re face of the nicotinamide ring.arrow_forward
- 8 The optimal temperature for the action of lactate dehydrogenase is 36°C. It is irreversibly inactivated at 85°C, but a yeast containing this enzyme can survive for months at —10°C. Explain how this can happen.arrow_forwardOne of the steps in the pentose phosphate pathway for glucose catabolism is the reaction of sedoheptulose 7-phosphate with glyceraldehydes 3-phosphate in the presence of a transaldolase to yield erythrose 4-phosphate and fructose 6-phosphate. (a) The first part of the reaction is the formation of a protonated Schiff base of sedoheptulose 7-phosphate with a lysine residue in the enzyme followed by a retro-aldol cleavage to give an enamine plus erythrose 4-phosphate. Show the structure of the enamine and the mechanism by which it is formed. (b) The second part of the reaction is a nucleophilic addition of the enamine to glyceraldehyde 3-phosphate followed by hydrolysis of the Schiff base to give fructose 6-phosphate. Show the mechanism.arrow_forwardWhich enzyme would catalyze the reaction illustrated below? triacylglycerol + 3H2O → glycerol + 3 fatty acids Group of answer choices a. sucrase b.galactosidase c. lipase d.peptidasearrow_forward
- GiventhatthechangeinGibbsfreeenergyforthehydrolysisofATPcorresponds to ∆rGm = −31 kJ mol-1 under the conditions prevailing in a typical cell, can the hydrolysis drive the formation of glutamine?arrow_forward3) The enzyme aldolase catalyzes the conversion of fructose-1,6-diphosphate (FDP)to dihydroxyacetone phosphate (DHAP) and glyceraldehide-3-phosphate (G3P). Thereaction isFDP ⇄ DHAP + G3P , ∆rG0(298.15 K) = 23.8 kJ mol−1In red blood cells the concentration of these species are [FDP] = 35 µM, [DHAP] =130 µM, and [G3P] = 15 µM. (Remember that 1.0 µM = 1.0 × 10−6 mol L−1. Thestandard state for reactions in solution can be taken as c0 = 1.0 mol L−1).Calculate ∆rG in a red blood cell at 25 0C. Will the reaction occur spontaneouslyin the cell at this temperature?arrow_forward
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