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.

Question

Want to see the full answer?

Answer 1

Question

Chapter 24, Problem 4P

Interpretation Introduction

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.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Students have asked these similar questions

Do schwann cells produce or act as myelin in the peripheral nervous system? I know that they encase and wrap around axons, but where does the myelin come into play?

The enzyme lactate dehydrogenase (LDH) catalyzes the conversion of pyruvate to lactatein skeletal muscle cells using NAD/NADH during anaerobic “balanced” fermentation.Answer the following questions about this reaction. (a) Write out the two reductive half reactions and indicate the E ̊' for each half reaction. Write out the full balanced reaction for the pyruvate to lactate rxn and indicate the ∆E ̊' for the reaction. (b) What is the free energy change under standard state conditions for thisreaction? Which direction is spontaneous?(c) Assume that in skeletal muscle cells the ratio of [NAD+] to [NADH] is 100, and that the[pyruvate] = 0.40 mM and [lactate] = 4.0 mM. What is the free energy change (∆G')for the conversion of pyruvate to lactate? Indicate the direction in which the reactionis spontaneous under these cellular conditions.

Why did the authors worry about the temperature-dependent solubility of the carriers in thebilayer? How did the authors determine whether the effect of freezing the lipid bilayer wasto decrease the solubility of the carriers (nonactin and valinomycin) or whether the effectwas to impair their ability to diffuse through the membrane (decrease their mobility)?