Enzymes
The proteolysis rate enhancement by chymotrypsin (~1010 folds) corresponds to a reduction in activation energy of about

58 kJ/mol
40 kJ/mol
49 kJ/mol
88 kJ/mol

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Enzymes
The cleavage specificity of trypsin and chymotrypsin depend in part on the

presence of a low-barrier hydrogen bond in the active site or specificity pocket
proximity of Ser 195 to the active site or specificity pocket
absence of water in the active site
size, shape, and charge of the active site or specificity pocket

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Enzymes
Before they can react, many molecules need to be destabilized. This state is typically achieved through

oxidizing the molecules by removing electrons
changing the reaction from a biosynthetic to a catabolic pathway
the input of a small amount of activation energy
changing the three-dimensional shape of the molecule

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Enzymes
Enzyme-driven metabolic pathways can be made more efficient by

concentrating enzymes within specific cellular compartments
grouping enzymes into free-floating, multienzyme complexes
fixing enzymes into membranes so that they are adjacent to each other
All of these

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Enzymes
In the enzyme-catalyzed reaction shown below, what will be the effect on substances A, B, C, and D of inactivating the enzyme labeled E2? A ---(E1)---> B ---(E2)---> C ---(E3)--->

A will still be produced, but not B, C, or D
A and B will still be produced, but not C or D
A, B, and C will still be produced, but not D
A, B, C, and D will all still be produced

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