Closely related. Pyruvate dehydrogenase complex and a-ketoglutaratea-ketoglutarate dehydrogenase complex are huge enzymesconsisting of three discrete enzymatic activities. Which amino acidsrequire a related enzyme complex, and what is the name of theenzyme?

Enzymes are biological catalysts that help in catalyzing or speeding up biological reactions by…

Answered: Closely related. Pyruvate dehydrogenase…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter25: Nitrogen Acquisition And Amino Acid Metabolism

Section: Chapter Questions

Problem 12P

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. Pyruvate can be processed under anaerobic conditions to ethanol (in yeast) or to lactate (in mammals), as shown. Explain the primary purpose of these reactions. Describe the major biochemical features of each reaction
Help filling in the blanks: The malate aspartate shuttle plays many roles in carbohydrate and amino acid metabolism. Malate can be transferred into the cytosol and interconverted in one enzymatic step to produce [oxaloacetate/glucose/PEP/pyruvate] for use in the pathway of [glycolysis/gluconeogenesis]. A product of the urea cycle, derived from aspartate, can also be converted to malate in one enzymatic step and shuttled into the mitochondria so that the urea cycle product can be used in [fatty acid synthesis/the citric acid cycle/β-oxidation]. The amino group from aspartate can be transferred to [oxalacetate/malate/fumarate/pyruvate/a- ketoglutarate] to form glutamate, which is then transported into the mitochondria. In fact many amino acids are transaminated in this way to form glutamate in the cytosol. In this way, incoming amino acids from the bloodstream can be shuttled into the liver mitochondria as glutamate for conversion by glutamate dehydrogenase to [glutamate/a-ketoglutarate…
Compare and contrast Pyruvate Dehydrogenase with a-ketoglutarate dehydrogenaseOutline the mechanisms of both enzymes. Discuss the functions of the coenzymes. List the similarities and the differences between the 2 enzymes. Both are very large membrane bound complexes. What are the advantages of this strategy?How detailed is the enzyme structure known below(It's Pyruvate Dehydrogenase )? What insight(s) does this structural detail give you about the enzyme mechanism.
G. ENZYME CLASSIFICATION. Identify the main class of enzymes used to catalyzed the following reactions: 1. Lactate dehydrogenase: NADH+H NAD HC-OH CH3 CH Pynnte Lactate 2. Methylmalonyl-CoA mutase: CH CH SCOA CH,CH, SCOA coenzyme B12 COO COO methylmalonyl-CoA succinyl-CoA 3. Enolase: 0. H–Ċ–0–P–0- C-0–P-0- + H,0 HO–CH, CH 6 Phosphoenolpyruvate 2-Phosphoglycerate 4. Chymotrypsin: -0–CH,CH3 + H2O - RCOOH + HOCH,CH3 5. Pyruvate carboxylase: coo • co, • ATP + H,0 H-C-H . ADP + P, + 2H čoo CH, Pyruvate Oxaleacetate
Palmitoleic acid, 16:1Δ⁹ hexadecaenoic acid, (16 carbon FA with one double bond )is an important fatty acid component of TAGs and cell membranes. Briefly explain the process of beta oxidation of this fatty acid and the number (only) of FADH, NADH and acetyl CoA outcome. What is the total ATP (only number) generated from this fatty acid after beta oxidation.
Instructions. Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described. Name: citryl-CoA synthetase Reaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA Name: D-xylulose reductase Reaction: xylitol + NAD+ = D-xylulose + NADH + H+ Name: cellobiose phosphorylase Reaction: cellobiose phosphate = α-D-glucose 1-phosphate + D-glucose Name: carbonic anhydrase Reaction: H2CO3 = CO2 + H2O Other info: The enzyme catalyzes the reversible hydration of gaseous CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH. Name: pantoate activating enzyme Reaction: ATP + (R)-pantoate = AMP + diphosphate + (R)-pantothenate.
Draw Gluconeogenesis. Please make sure to state all the enzymes and co-factors for each step of the pathway.
A. The inhibitor constants for three inhibitors of por- cine citrate synthase are summarized in the table on the right. The compounds were all determined to bind in the active site as competitive inhibitors of acetyl-CoA. Because they bind as competitive inhibitors, all three inhibitors must exhibit structural similarity to some part of acetyl-CoA. Look up in the textbook the structural formu- las for Coenzyme A, ATP, and NADH. What is the largest structural fragment of each inhibitor that is responsible for competitive inhibition? Draw the molecular fragment common to each inhibitor that competes with the binding of acetyl-CoA in the active site of citrate synthase. Bromoacetyl-CoA ATP NADH K₁ (μM) 25.7 6800 8300 B While the inhibitor constants listed in part (b) above were determined in vitro for purified citrate synthase, does their inhibitory action have any relevance to the flux of metabolites through the TCA cycle in vivo? If so, explain.
X INCORRECT; see section 13.1 Enzymes occasionally display weak "“side" activities. Draw the structure of the product (other than ADP) of the reaction that results when pyruvate kinase, operating in reverse, uses lactate as a substrate. For your structure: 1. Do not include primary or secondary hydrogens. CH2 HO OH Edit Drawing
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Calculate the total number of ATP that can be generated from the ß-oxidation of paulinic acid? ОН 1. How many ATP expended for activating fatty acid to fatty acyl-CoA? How many rounds of beta oxidation? How many FADH2 per round of beta oxidation? Is there any point in the beta oxidation of an unsaturated fatty acid where we skip over FADH, production? How many FADH, total from beta oxidation? How many NADH per round of beta oxidation? How many NADH total from beta oxidation? How many acetyl-CoA are produced through beta oxidation? 6. 2. 3. 4. 5. How many NADH and FADH, are produced per acetyl-CoA in the citric acid cycle? How many NADH total from all acetyl-CoA running through the citric acid cycle? How many FADH, total from all acetyl-CoA running through the citric acid cycle? How many ATP are produced per acetyl-CoA in the citric acid cycle? How many ATP total from all acetyl-CoA running through the citric acid cycle? How many ATP per NADH,? 9. 7. 1. 8. How many ATP per FADH,? 10.…
- Outline the mechanism of the conversion of a-ketoglutarate to succinyl- CoA catalyzed by a-ketoglutarate dehydrogenase complex. Include all products, coenzymes, and reactions in your discussion.

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Closely related. Pyruvate dehydrogenase complex and a-ketoglutarate a-ketoglutarate dehydrogenase complex are huge enzymes consisting of three discrete enzymatic activities. Which amino acids require a related enzyme complex, and what is the name of the enzyme?