Biochemistry
Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
Question
Book Icon
Chapter 22, Problem 59P
Interpretation Introduction

(a)

Interpretation:

The effect of soraphen A and its varying concentration on the fatty acid synthesis should be determined.

Concept introduction:

Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme, which catalyzes the conversion of acetyl-CoA into malonyl-CoA, in the presence of bicarbonate ion. It has two catalytic activities, carboxyltransferase and biotin carboxylase. This enzyme is found in the chloroplasts of the plants, and endoplasmic reticulum of the animals. The main motive of ACC is to synthesize malonyl CoA for the synthesis of fatty acids.

Interpretation Introduction

(b)

Interpretation:

The effect of soraphen A on fatty acid oxidation must be determined.

Concept introduction:

Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme, which catalyzes the conversion of acetyl-CoA into malonyl-CoA, in the presence of bicarbonate ion. It has two catalytic activities, carboxyltransferase and biotin carboxylase. This enzyme is found in the chloroplasts of the plants, and endoplasmic reticulum of the animals. The main motive of ACC is to synthesize malonyl CoA for the synthesis of fatty acids.

Interpretation Introduction

(c)

Interpretation:

The results of graph B should be explained keeping in mind that sorpahen A inhibits acetyl CoA carboxylase.

Concept introduction:

Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme, which catalyzes the conversion of acetyl-CoA into malonyl-CoA, in the presence of bicarbonate ion. It has two catalytic activities, carboxyltransferase and biotin carboxylase. This enzyme is found in the chloroplasts of the plants, and endoplasmic reticulum of the animals. The main motive of ACC is to synthesize malonyl CoA for the synthesis of fatty acids.

Interpretation Introduction

(d)

Interpretation:

The effect on phospholipid synthesis by inhibition of carboxylase must be determined.

Concept introduction:

Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme, which catalyzes the conversion of acetyl-CoA into malonyl-CoA, in the presence of bicarbonate ion. It has two catalytic activities, carboxyltransferase and biotin carboxylase. This enzyme is found in the chloroplasts of the plants, and endoplasmic reticulum of the animals. The main motive of ACC is to synthesize malonyl CoA for the synthesis of fatty acids.

Interpretation Introduction

(e)

Interpretation:

The effect of phospholipid synthesis on cell’s viability must be determined.

Concept introduction:

Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme, which catalyzes the conversion of acetyl-CoA into malonyl-CoA, in the presence of bicarbonate ion. It has two catalytic activities, carboxyltransferase and biotin carboxylase. This enzyme is found in the chloroplasts of the plants, and endoplasmic reticulum of the animals. The main motive of ACC is to synthesize malonyl CoA for the synthesis of fatty acids.

Interpretation Introduction

(f)

Interpretation:

The result of soraphen A on cancer cell viability should be determined.

Concept introduction:

Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme, which catalyzes the conversion of acetyl-CoA into malonyl-CoA, in the presence of bicarbonate ion. It has two catalytic activities, carboxyltransferase and biotin carboxylase. This enzyme is found in the chloroplasts of the plants, and endoplasmic reticulum of the animals. The main motive of ACC is to synthesize malonyl CoA for the synthesis of fatty acids.

Blurred answer
Students have asked these similar questions
Tracing glucose. Glucose labeled with 14 C at C-6 is added to a solution containing the enzymes and cofactors of the oxidative phase of the pentose phosphate pathway. What is the fate of the radioactive label?
Inducers and Inhibitors of AEP. Short peptides such as legumain stabilization and activity modulation (LSAM) domain and αvβ3 integrin could enhance the activity of AEP. LSAM domain known as the prodomain of AEP blocks substrate binding before activation. This prodomain has a helical structure and two independent peptides. One is an activation peptide (AP, K287 to N323), and the other is a LSAM domain. LSAM domain remains even after AP is cleaved and released from protease at neutral pH via electrostatic interaction. AEP without LSAM domain has a lower melting temperature than AEP with LSAM domain [77, 117]. Another short peptide, αvβ3 integrin, can directly interact with AEP, and after forming a complex, the optimal pH for AEP activity is increased from 5.5 to 6.0. It indicates that αvβ3 binding could induce conformational stabilization of AEP accompanied by deprotonated C189. αvβ3 does not directly interact with the AEP active site; however, AEP docks to the αvβ3 RGD-binding site…
Required partner. Aminotransferases require which of the following cofactors: a. NAD+/NADP+NAD+/NADP+ b. Pyridoxal phosphate c. Thiamine pyrophosphate d. Biopterin
Knowledge Booster
Background pattern image
Similar questions
SEE MORE QUESTIONS
Recommended textbooks for you
  • Text book image
    Biochemistry
    Biochemistry
    ISBN:9781305577206
    Author:Reginald H. Garrett, Charles M. Grisham
    Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning