*OBJ - Enzymes as Biocatalysts Flashcards

1
Q

Interpret the energy diagram of an enzyme catalyzed reaction and an uncatalyzed reaction

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2
Q

Define activation energy and its relationship with the transition state complex formation

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3
Q

Define binding energy and describe its importance in enzyme catalyzed reactions

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4
Q

Define transition state, and explain how structural information on the transition state of a reaction can be exploited in drug development

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5
Q

Distinguish between the lock-and-key model and the induced-fit model for substrate binding

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6
Q

Describe the active site of chymotrypsin, and explain the major chemical steps leading to peptide bond cleavage

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7
Q

Identify the specific roles of the active site amino acid residues involved in the peptide bond cleavage

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8
Q

Distinguish between catalytic transition state and catalytic intermediates and identify their positions in the energy diagram of a given enzyme-catalyzed reaction

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9
Q

List the functional groups commonly encountered in the active sites of enzymes.

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