FUNDAMENTALS OF BIOCHEMISTRY-ACCESS
FUNDAMENTALS OF BIOCHEMISTRY-ACCESS
5th Edition
ISBN: 9781119498742
Author: Voet
Publisher: WILEY
Question
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Chapter 15, Problem 35CQ

(a)

Summary Introduction

To match: The enzyme galactose dehydrogenase with reaction given for the ascorbic acid biosynthesis pathway.

Concept introduction: Ascorbic acid is also known as L-ascorbic acid, which is a vitamin C element as well as an antioxidant. Galactose dehydrogenase is an enzyme that belongs to oxidoreductase family of enzyme. This especially acts on the CH-OH donor group.

(b)

Summary Introduction

To explain: The enzyme GDP-D-mannose-3, 5-epimerase with reaction given for the ascorbic acid biosynthesis pathway.

Concept introduction: The ascorbic acid is also known as L-ascorbic acid, which is a vitamin C element as well as an antioxidant. The enzyme GDP-D-mannose-3, 5-epimerase is an enzyme of isomerase family.

(c)

Summary Introduction

To explain: The enzyme phosphoglucose isomerase with reaction given for the ascorbic acid biosynthesis pathway.

Concept introduction: Ascorbic acid is also known as L-ascorbic acid, which is a vitamin C element as well as an antioxidant. Phosphoglucose isomerase is the isomerase enzyme.

(d)

Summary Introduction

To explain: The enzyme phosphomannose isomerase with reaction given for the ascorbic acid biosynthesis pathway.

Concept introduction: Ascorbic acid is also known as L-ascorbic acid, which is a vitamin C element as well as an antioxidant. The enzyme phosphomannose isomerase is the facilitating enzyme that interconverts two molecules.

(e)

Summary Introduction

To explain: The enzyme phosphomannose mutase with reaction given for the ascorbic acid biosynthesis pathway.

Concept introduction: The ascorbic acid is also known as L-ascorbic acid, which is a vitamin C element as well as an antioxidant. The enzyme phosphomannose mutase is a catalytic enzyme.

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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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FUNDAMENTALS OF BIOCHEMISTRY-ACCESS

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