EBK LEHNINGER PRINCIPLES OF BIOCHEMISTR
EBK LEHNINGER PRINCIPLES OF BIOCHEMISTR
7th Edition
ISBN: 8220103662253
Author: nelson
Publisher: MAC HIGHER
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Chapter 13, Problem 19P

(a)

Summary Introduction

To determine: The general type of enzyme and cofactor(s) or reactants required during dehydrogenation reactions that would result in the formation of the product.

Introduction:

The fats disintegrate into fatty acids and glycerol. The fatty acids enter Krebs’s cycle and get involved in beta-oxidation where its carbons are removed and acetyl CoA (acetyl coenzyme A) are formed. The cholesterol molecules are formed by the utilization of acetyl CoA molecules.

(b)

Summary Introduction

To determine: The general type of enzyme and cofactor(s) or reactants required in isomerization of L- and D- leucine..

Introduction:

The amino acids are the building blocks of the macromolecules proteins. There are twenty amino acids required to make proteins in all organisms. These proteins participate in the metabolism of organisms.

(c)

Summary Introduction

To determine: The general type of enzyme and cofactor(s) or reactants required in interconversion of glucose and fructose.

Introduction:

The sugars are carbohydrates that include monosaccharides and disaccharides. The sugars include glucose, sucrose, fructose, maltose, and many more sugars. The sugars are interconvertible and get converted into glucose. The glucose enters glycolysis and generates cellular energy in terms of ATP (Adenosine triphosphate).

(d)

Summary Introduction

To determine: The general type of enzyme and cofactor(s) or reactants required in the phosphorylation of glycerol to glycerol-3-phosphate.

Introduction:

The digestive products of the fats are “glycerol” and “fatty acids”. The lipase acts on the fat molecules and, the fatty acid and glycerol molecules are formed. The fats are digested in the small intestine.

(e)

Summary Introduction

To determine: The general type of enzyme and cofactor(s) or reactants required for hydrolysis of a peptide bond.

Introduction:

The proteins are formed by repeated linkage of amino acids through peptide bonds. The amino acids have “carboxyl group”, “amino group” and “R group”. The two amino acids are joined by peptide bond, such that the carboxyl group of one amino acid reacts with amino group of another amino acid. This result in formation of peptide bond and water molecule is lost.

(f)

Summary Introduction

To determine: The general type of enzyme and cofactor(s) or reactants required for the dehydrogenation of glycerol.

Introduction:

The digestive products of the fats are “glycerol” and “fatty acids”. The lipase acts on the fat molecules and the fatty acid and glycerol molecules are formed. The fats are digested in the small intestine.

(g)

Summary Introduction

To determine: The general type of enzyme and cofactor(s) or reactants required for reduction of acetaldehyde.

Introduction:

The liver performs several functions important for bodily processes. The damage done to liver affects several functions of body that includes lipids, carbohydrates, and proteins metabolism.

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Students have asked these similar questions
The beta-lactamase hydrolyzes the lactam-ring in penicillin. Describe the mechanism  of hydrolysis, insuring to include the involvement of S, D, & K in the reaction sequence. Please help
To map the active site of beta-lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Why doesn't D in this hexapeptide not participate in the hydrolysis of the beta-lactam ring even though S, K, and D are involved in the catalyst?
To map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine.  Using the experimental results described above derive the primary sequence of the active site hexapeptide. Please help!
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