15-ACP0 tenslonilmalonyl-Acpen geno moil gritate20Tomore mdeulles of•S-ACPSH✓NDuORH3. reduction H₂2. dehydration (14)A reductionS-ALPmalonyl-coAHA2:05 bios siasatmoqueose to aizonturyzoid or to switch or two wordvdisqit as low an atouborq bas atost ile to autoute ori wod2 lozotyo ni ao ti asen most woda ob tudoto.A00 AM TA to zetourte od warb of boon ton ob woYameinsfloor ortTous disof+ del-Sn ob uoYsensiq staingonqqa oli niS-содtilacetyl-cAS-WAebysces kon go wiS-COAИзtila maldo19C3=H3C14synthase. Show where the radio labels will appear in palmitate (16:0)Unlabeled malonyl-CoA and the following radio labeled acetyl-CoA were used as substrates for fatty acidProblem 5 Phosphate Problem 5• Unlabeled malonyl-CoA and the following radio labeled acetyl-CoA were used as substrates for fatty acidsynthase. Show where the radio labels will appear in palmitate (16:0)H3C14ACBLOP GUS-COAw tнеS-COAH3C.acetyl w AH₂₂ 14 S-ACP +acetyl Acpmalonyl.coAokSCOA=-S-ACPmalonyl-Acpreduction2. dehydration3 reduction-102Dumitrups (100)hundpalmitateH₂CODA COY MGLC 14H₂01₂014s-Acp6 more moleules of malonyl Acp√16neS- ACP

Fatty acids are used to store energy and are crucial parts of cell membranes. The production of…

Answered: ● Unlabeled malonyl-CoA and the…

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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Order the cofactors based on their use in the mechanism of the a-etogluterate dehydrogenase complex. 1. Stabilizes a carbanion due to decarboxylation 2. Allows for the splitting of the carbon skeleton from the electron pair generated in a redox reaction 3. Enzyme bond electron carrier that is part of dihydrolipoyl dehydrogenase 4. Final electron acceptor in the overall reaction catalyzed by this complex 1 2 3 4 answer choices: lipoamide, biotin, 2 Fe - 2S cluster, TPP, NAD+, FAD
Lactate dehydrogenase is a tetramer of MW 134000 g/mole composed of subunits which are equal in size. It is found in the cytoplasm of eukaryotic and prokaryotic cells. Describe the secondary, tertiary and quaternary structures of lactate dehydrogenase.
The mechanism of chymotrypsin can be viewed as a two-step process, acylation of the enzyme active site followed by a deacylation reaction. What accounts for the observed "burst" in rapid kinetic studies of the hydrolysis of N-acetyl-L-phenylalanine p-nitrophenyl ester by chymotrypsin? The rate of hydrolysis of the acyl-enzyme intermediate is faster than the rate of forming the acyl-enzyme intermediate. The rates of the acylation and deacylation reactions are equal. The rate of the acylation reaction is slower than the rate of the deacylation reaction. The rate of the acylation reaction is faster than the rate of the deacylation reaction.
25. The AG" values for the two reactions are given. 1. 2. oxaloacetate + acetyl-CoA + H₂O → citrate + COASH oxaloacetate + acetate → citrate Enzymes for reactions 1 and 2 are citrate synthase and citrate lyase, respectively. Determine the AG" for the hydrolysis of acetyl-CoA acetyl-CoA + H₂O acetate + COASH + H+ plane een isoimorfbold bns (94) opg Vp1903 9911 AG¹⁰ ? AGO = -32.2 kJ/mol AG"=-1.9 kJ/mol
The KM values for the reaction of chymotrypsin with two different substrates are given in the table below. Considering this information, which substrate has the lower apparent affinity for the enzyme? Which substrate is likely to give a lower value for Vmax? Substrate N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester KM (M) 8.8 X 10-² 6.6 X 10-4 N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give a lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give the lower V₁ max. N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; N- acetyltyrosine ethyl ester is likely to give the lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; N- acetylvaline will likely to give the lower Vmax. None of the above statements are correct.
Based on the image below, select the correct statements. Note: There may be more than 1 correct response. Ribose 5-phosphate ribose phosphate pyrophosphokinase (PRPP synthetase) glutamine-PRPP amidotransferase adenylosuccinate synthetase AMP -> PRPP 5-Phosphoribosylamine I adenylosuccinate lyase 9 steps Adenylosuccinate AMP IMP <-- ADP <- AMP <-- GMP <-- IMP IMP dehydrogenase <- GMP. XMP ADP ATP XMP-glutamine amidotransferase GMP يا Increased levels of ADP inhibit the production of PRPP. Increased levels of GMP inhibit the production of XMP. Increased ADP activates PRPP synthase to increase PRPP levels. Increased IMP activates glutamine-PRPP amidotransferase to further increase IMP levels.
Explain why step 1 of the citric acid cycle is inhibited by succinyl-CoA. Be complete for full credit.
The mitochondrial form of carbamoyl phosphate synthetase is allosterically activated by N-acetylglutamate. Briefly describe a rationale for this effect.
The purinosome contains enzymes that convert the serine hydroxymethyl group to the formyl group of 10-formyltetrahydrofolate. Write a balanced equation for each reaction in this conversion.
Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Chymotrypsin Ки (М) 4.4 x 10-1 8.8 x 10-2 6.6 x 104 Kcat (S-1) 5.1 x 10-2 1.7 x 10-1 1.9 x 102 Substrate N-acetylglycine ethyl ester N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 OA. N-acetylglycine ethyl ester OB. N-acetylvaline ethyl ester OC. N-acetyltyrosine ethyl ester D. Urea
Consider the hypothetical reaction plot of salivary α-amylase shown below: a. Determine whether the plot describes substrate disappearance or product formation. Using Equation 5-2, express the rate of reaction described by the plot.b. Based on the plot, determine the time interval at which the rate of reaction must be measured.
Identify the enyme

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● Unlabeled malonyl-CoA and the following radio labeled acetyl-CoA were used as substrates for fatty acid synthase. Show where the radio labels will appear in palmitate (16:0)