Arrange the steps of breakdown of oleic acid (pictured below) in the correct order.12345activation by acyl-CoAsynthe ✓[Choose ]one cycle ofß-oxidationbeginning at the enoyl-CoAhydratasestepthree cycles ofẞ-oxidationfive cycles ofß-oxidationactivation by acyl-CoAsynthetaseenoyl-CoAisomeraseactivityenoyl-CoAisomeraseactivity Vone cycle ofß-oxidationbegini Vfive cycles ofß-oxidationOH

Beta oxidation: The enzyme fatty acyl-CoA synthase (FACS) adds a CoA group to the fatty acid chain…

Answered: Arrange the steps of breakdown of oleic…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 18P: Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in...

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Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.
Radiolabeling with 14C-Glutamate Describe the labeling pattern that would result from the introduction into the TCA cycle of glutamate labeled at Cy with 14C.
GTP or ATP is produced during the conversion of isocitrate into ketoglutarate succinyl CoA into succinate fumarate into malate malate into oxaloacetate
The peroxisomal enzyme b-ketoacyl–CoA-thiolase does notbind medium-chain acyl-CoA, in contrast to the analogousmitochondrial enzyme. Explain why this phenomenon is anadvantage to the cell.
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
uizzes/67365/take Based on the image below, select the correct statements. Note: There may be more than 1 correct response. I Ribose 5-phosphate ribose phosphate pyrophosphokinase (PRPP synthetase) glutamine-PRPP amidotransferase adenylosuccinate synthetase AMP > 5-Phosphoribosylamine I adenylosuccinate PRPP lyase 9 steps Adenylosuccinate AMP IMP <-- ADP - AMP <-- GMP <-- IMP IMP dehydrogenase <- GMP - XMP ADP ATP GMP يمد XMP-glutamine amidotransferase Increased levels of ADP inhibit the production of PRPP. Increased levels of GMP inhibit the production of XMP. O Increased ADP activates PRPP synthase to increase PRPP levels. Increased IMP activates glutamine-PRPP amidotransferase to further increase IMP levels. 8 OBC
Glucosidase I catalyzes hydrolysis of specific glucosidase I is a synthetic trisaccharide, glucose-al-2- glucose-al-3-glucose-a-O(CH₂) #COOCH3. Kinetic measurements oligosaccharides containing glucose. obtained using this trisaccharide as substrate in the deoxynorjirimycin at concentrations of 50 μM (), 100 μM absence (x-x) and presence of the inhibitor 1- A) were used to prepare the (-), and 200 μM (4 Lineweaver-Burk plot below: b) Page 3 12) 7. a) V/V (nmol/hr)-1 1.S 1.0- 0.5 1/Trisaccharide (mM)-! Estimate the values for Vmax and KM for the trisaccharide substrate in the absence of the inhibitor. 0.0 -1.0 0.0 One substrate for 1.0 2.0 Determine whether inhibition by 1-deoxynorjirimycin is competitive, non-competitive or neither.
Incubation of the norsolinic acid synthase holo-ACP with malonyl CoA gave malonyl-S-ACP (molecular weight 10112 Da). (ACP SH holo-ACP Malonyl-SNAC Calculate the molecular weight of holo-ACP. (ACP OH malonyl-S-ACP MW = 10112
Draw the products of the reaction of xylulose-5-phosphate and erythrose-4-phosphate catalyzed by transketolase in the pentose phosphate pathway. Provide the structure in the protonation state found in physiological conditions. H H H OH FO HO-H H-OH H OPO3²- Q transketolase Draw glyceraldehyde-3- phosphate H H- H H H O OH OH OPO3²- Draw fructose-6- phosphate Q I I
Can you give me more expalination of Oxidation Deamination formation of -ketoglutaric acid and NH4+ from glutamate in the presence of glutamate dehydrogenase What is the rule for glutamate to oxaloacetate to form α-ketoglutarate and aspartate?
When the identical subunits of chicken liver fatty acid synthase are dissociated in vitro, all of the activities can be detected in the separated subunits except for the β-ketoacyl synthase reaction and the overall synthesis of palmitate. Explain these observations.
Describe the roles of dUTPase, thymidylate synthase, and dihydrofolate reductase in the synthesis of dTMP.

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