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Chapter 10, Problem 13P
Summary Introduction

To determine: The cleavage products of PIP2 by phospholipase C.

Introduction: Phosphatidylinositol 4,5-bisphosphate ( PIP2 ) is an essential lipid that is integral to the plasma membrane of the plant and animal cells. It works as a second messenger in a various signaling pathways and also involved in metabolic processes. PIP2 is an important phosphoinositide that makes about 1% of the cell membrane. PIP2 is also involved in the signaling transduction of the extracellular or intracellular components.

Summary Introduction

To compare: The DAG and IP3 with respect to their properties and solubilities in water.

Introduction: DAG and IP3 are the products of the hydrolysis of PIP2 by the enzyme phospholipase C. DAG pathway is a signaling transduction pathway that is involved in the activation of enzymes. IP3 molecule is the negatively charges polar molecule. IP3 involved in the signaling transduction of chemicals such as growth factors, hormones, and neurotransmitters.

Summary Introduction

To predict: Whether either would diffuse readily through the cytosol.

Introduction: DAG and IP3 are the products of the hydrolysis of PIP2 by the enzyme phospholipase C. DAG pathway is a signaling transduction pathway that is involved in the activation of enzymes. IP3 molecule is the negatively charges polar molecule. IP3 involved in the signaling transduction of chemicals such as growth factors, hormones, and neurotransmitters.

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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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