1. Choose all the correct answers. Enzyme catalyzing this reaction:COOCO0ноC-H+ NAD*CH2+ NADH + H*CH2лвенныйтетCoOCOOL-MalateOxaloacetateA. Belongs to the class of transferases.B. Belongs to the class of oxidoreductases.C. Is a simple enzyme.D. Is a holoenzyme. 2. Parkinson's disease is caused by a deficiency of dopamine in the substantia nigra of thebrain. Dopamine is produced in the brain from L-DOPA (L-dihydroxyphenylalanine)by removal of a molecule of carbon dioxide. The L-DOPA is produced by oxidation oftyrosine, which is in turn produced from phenylalanine by another oxidoreductase. Theenzyme that converts L-DOPA to dopamine is best classified as an/a:A. Oxidoreductase.B. Transferase.C. Hydrolase.D. Lyase.E. Isomerase.3. Most synthetic reactions in which carbon dioxide is used reguire the vitamin biotin. The200yniCenen

Enzymes are actually classified into seven classes, namely oxidoreductases, transferases,…

Answered: 2. Parkinson's disease is caused by a…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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2. 'a) List the number of NADH and FADH2 equivalents formed and the corresponding number or ATP equivalents generated by mitochondrial oxidation of one molecule of CH3(CH2)12-COSCOA Number of NADH or Number of ATP Enzyme catalyzing the oxidation step FADH, formed ultimately formed B Oxidation Acyl-CoA dehydrogenase B-Hydroxyacyl-CoA dehydrogenase Citric acid cycle Isocitrate dehydrogenase a-Ketoglutarate dehydrogenase Succinyl-CoA synthetase Succinate dehydrogenase Malate dehydrogenase Total "These calculations assume that mitochondrial oxidative phosphorylation produces 1.5 ATP per FADH2 oxidized and 2.5 ATP per NADH oxidized. "GTP produced directly in this step yields ATP in the reaction catalyzed by nucleoside diphosphate kinase (p. 516). For all of the questions below, assume that respiratory activity of mitochondria is supported by CH3(CH2)12-COSCOA in the presence of excess ADP (+ P). (b) How many ATP equivalents will be generated in the presence of the inhibitor rotenone? Give a…
a. In the TCA cycle, which of the following combines with acetyl CoA to form a 6-carbon compound? i. oxaloacetate ii. thiamine iii. glucose iv. pyruvate b. The last step in glycolysis is the transfer of phosphoryl group from phosphoenolpyruvate to ADP catalyzed by pyruvate kinase. i. True ii. False
3. Acetylcholinesterase is a serine hydrolase enzyme im- portant in nerve signal transmission, hydrolyzing acetylcho- line, an ester molecule with a positively charged quaternary nitrogen group. The structure of the physiologically relevant substrate of this enzyme is shown on the right. The quater- H₂C nary nitrogen group serves to anchor the molecule in the active site Gly121 Oxy- anion hole Gly122 Ala204 Substrate ACh His447 Catalytic triad Ser203 Glu202 Glu334 Ser229 CH3 N+ CH3 CH3 The a Scale document down rine protease family, consisting of a catalytic triad Ser203- His447-Glu334 with Ser203 supplying the nucleophilic hydroxyl group and an oxyanion hole com- prised of peptide NH groups of Gly121, Gly122, and Ala204, illustrated in the diagram above, for which carbon (green), nitrogen (blue), and oxygen (red) atoms are shown while hydrogen atoms are white. The enzyme catalyzed reaction can be represented by the following scheme: (a)( k1 K2 E + S = ES K-1 K3 EYE + P where ES…
3. Calculate the ATP that is produced when linoleic acid (9,12-octadecadienoic acid; 18:2) is (a) oxidized to CO2 and H20 or (b) converted to the ketone body acetoacetate in the liver and then oxidized to CO2 and H20 in the peripheral tissues. 4. Explain the role of AMP-dependent protein kinase in regulating fatty acid metabolism. What are the ways hormonal control of fatty acid metabolism works between fed and fasted states? Please draw by hand/digitally, schematics showing this regulation in adipose tissue, muscle and liver.
. Propose a mechanism for the reaction catalyzed by dopamine B-hydroxylase. Assume that copper in the enzyme binds O, and that copper can change its oxidation state during the reaction.
which statements are False?
36. In the conversion of pyruvate to acetyl CoA, - an acetyl group is transferred to Coenzyme A to produce acetyl CoA. - only one pyruvate molecule loses one carbon atom with the release of carbon dioxide. - the succinate dehydrogenase complex requires four coenzymes. - electrons are transferred to NADH to produce NAD*.
3. Aspartate aminotransferase (AspAT) catalyzes the following reaction: COO™ C=O CH₂ COO Oxaloacetate The AspAT enzyme has two active-site arginines, Arg 386 and Arg 292, that interact with the a- carboxylate and ß-carboxylate groups on the aspartate substrate, respectively. Investigators stud- ied the mechanism of AspAT in more detail by constructing mutant AspAT enzymes in which either or both of the essential arginines were replaced with a lysine residue. The kinetic parame- ters for the wild-type enzyme and nutant enzymes are shown in the table. NH—CH-COO T CH₂ COO™ Aspartate α-Amino acid Enzyme 1. Wild-type Asp AT(Arg 292 Arg 386) 2. Mutant Asp AT(Lys 292 Arg 386) 3. Mutant Asp AT(Arg 292 Lys 386) 4. Mutant Asp AT(Lys 292 Lys 386) Asp-AT a-Keto acid KM (MM) 4 326 72 300 Kcat (S-1) 530 4.5 9.6 0.055 (a) The Michaelis constant is strictly not equivalent to an equilibrium binding constant; however under certain conditions the Michaelis constant does approach the equilibrium (dissoci-…
4. Fatty acid COA esters are unable to diffuse through the inner mitochondrial membrane. Thus, transport through the inner membrane is cataylyzed by , a separate a two enzymes carnitine acyltransferase 1, and carnitine acyltransferase II? Why do we need two enzymes and not only one.
2. A 4-year-old girl was diagnosed with thiamine deficiency and the symptoms include tachycardia, vomiting, convulsions. Laboratory examinations reveal high levels of pyruvate, lactate and a-ketoglutarate. Explain which coenzyme is formed from vitamin B, and its role in oxidative decarboxylation of pyruvate. For that: a) describe the structure of pyruvate dehydrogenase complex (PDH) and the cofactors that it requires; b) discuss the symptoms which are connected with the thiamine deficiency and its effects on PDH and a-ketoglutarate dehydrogenase complex; c) explain the changes in the levels of mentioned metabolites in the blood; d) name the deseribed discase,
1. Opine dehydrogenases (ODH) have evolved in invertebrate marine organisms with wide-ranging physiological roles. The first class of this family of enzymes provides an alternative pathway for the lactate dehydrogenase pathway in anaerobic energy production. The lactate dehydrogenase pathway is found in higher organisms and in mammals including humans. One class of opine dehydrogenases catalyzes the reductive coupling of pyruvate to N-a-carboxyalkyl-L-amino acids represented by the re- action below: དང་ NH₂ ODH ས HO S མིནྟཱ ཨཱར པ 'ནཔི ཏཏྭཱ ཡཾ དསྨཱ ཨབྷིནྡནྟི ཨཱ R₂ OH NAD(P)H NAD(P)* R OH R₁ R₂ where R1 is the side chain of the amino acid, R2 represents the alkyl group of the a-keto acid that is coupled to the amino acid, and NAD(P)H/NAD(P)* are the reduced/oxidized forms of nicotinamide ad- enine dinucleotide phosphate, a cofactor of the enzyme that catalyzes oxidation-reduction reactions. (a). : The product of the reaction has two chiral centers as shown: The Ca atom of the amino acid…
1. Opine dehydrogenases (ODH) have evolved in invertebrate marine organisms with wide-ranging physiological roles. The first class of this family of enzymes provides an alternative pathway for the lactate dehydrogenase pathway in anaerobic energy production. The lactate dehydrogenase pathway is found in higher organisms and in mammals including humans. One class of opine dehydrogenases catalyzes the reductive coupling of pyruvate to N-a-carboxyalkyl-L-amino acids represented by the re- action below: NH₂ ི་ ODH HO R 요 OH སྨིཾནྟཱ ར པ དརཱ ཨཱཋཏྭཱ… … ཨཱསྨིཾ ཏྟཏྟིནྡནྟི ཨཱ HO NAD(P)H NAD(P)* S R₁ R₂ where R1 is the side chain of the amino acid, R2 represents the alkyl group of the a-keto acid that is coupled to the amino acid, and NAD(P)H/NAD(P)* are the reduced/oxidized forms of nicotinamide ad- enine dinucleotide phosphate, a cofactor of the enzyme that catalyzes oxidation-reduction reactions. (a). The product of the reaction has two chiral centers as shown: The Ca atom of the amino acid…

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