Concept explainers
Interpretation:
A maximal separation between the malonyl transferase and the β-ketoacyl-ACP synthase active sites should be estimated.
Concept Introduction:
Fatty acid synthase is a multi-enzyme protein which catalyzes the fatty acid biosynthesis.Major function is catalyzing the formation of palmitate from acetyl CoA and malonyl CoA. Mammalian fatty acid synthase contains two identical protein subunits. Three catalytic domains are in N-terminal section which are β-ketoacyl-ACP synthase, malonyl/acetyl transferase and dehydrase. Four catalytic domains are in C-terminal section, which are enoyl reductase, ketoacyl reductase, acyl carrier protein and thioesterase. N terminal section and C terminal section is separated by 600 residues.
Want to see the full answer?
Check out a sample textbook solutionChapter 24 Solutions
Biochemistry
- Regulation of Glutamine Synthetase by Covalent Modification Suppose at certain specific metabolite concentrations in vivo the cyclic cascade regulating E. coli glutamine synthetase has reached a dynamic equilibrium where the average state of GS adenylylation is poised atn=6. Predict what change in nwill occur if: [ ATP ] increases, PIIA/PIID increases, [ -KG ]/[ Gln ] increases, [ Pi ] decreases.arrow_forwardModeling the Regulation of AcetyI-CoA Carboxylase Based on the information presented in the text and in Figures 24.4 and 24.5, suggest a model for the regulation of acetyl-CoA carboxylase. Consider the possible roles of subunit interactions, phosphorylation, and conformation changes in your model.arrow_forwardUsing the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.arrow_forward
- MATHEMATICAL Calculate the net ATP yield from the complete processing of a saturated fatty acid containing 17 carbons. Consider the -oxidation steps, processing of acetyl-CoA through the citric acid cycle, and electron transport.arrow_forwardRadiotracer Labeling of Pyruvate from Glucose Determine the anticipated location in pyruvate of labeled carbons If glucose molecules labeled (in separate experiments.) with 14C at each position of (.tie carbon skeleton proceed through the glycolytic pathway.arrow_forwardExtending the Mechanism of Methylmalonyl-CoA Mutase to Similar Reactions Based on the mechanism for the methylmalonyl-CoA mutase (see problem 14), write reasonable mechanisms for the following reactions shown.arrow_forward
- 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.arrow_forwardApproximately how much does staphylococcal nuclease (Table) decrease the activation free energy ΔG‡ of its reaction (the hydrolysis of a phosphodiester bond) at 25°C?arrow_forward9arrow_forward
- The Payoff Phase of Glycolysis in Skeletal Muscle In the skeletal muscle, in anaerobic conditions, glyceraldehyde 3- phosphate is converted into pyruvate during the payoff phase of glycolysis; and this pyruvate is reduced into lactate during lactic fermentation. 1-Write the 11 balanced biochemical equations corresponding to all| the reaction steps leading to the conversion of glyceraldehyde-3- phosphate into lactate through glycolysis followed by lactic fermentation. 2-Write the net equation of the whole transformation process (i.e. with glyceraldehyde-3-phosphate as the starting substrate; and lactate as the end product).arrow_forwardMake an electron-flow-mechanism for this synthetic scheme. This involves predicting major and by-products using electronic and structural effects. The arrow push mechanism must be shown.(from the reaction of α-ketoacids and oxaprolines to proteins that contain native serine residues ) with labelarrow_forwardPlease help!arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning