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PHS 912: Sept 29

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1.
1 point
During _________ Acid-Base Catalysis, the catalytic group participates in proton transfer which stabilizes the transition state.
2.
1 point
During ________ Acid-Base Catalysis, protons from amino acid side chains, cofactors, and organic substrates act as acid and base groups.
3.
1 point
Enzymes affect the equilibrium of reactions.
4.
1 point
Substrates are most tightly bound when in the highest energy level.
5.
1 point
In __________ catalysis, rate acceleration occurs through transient formation of an enzyme-substrate covalent bond.
6.
1 point
If the enzyme functions as an acid, it needs to function as a base later.
7.
1 point
__________ catalysis often participates in oxidation-reduction reactions.
8.
1 point
_________ utilize electrostatic interactions in the transition state to reduce the activation energy.
9.
1 point
Name the 7 amino acids that can function in covalent catalysis.
10.
1 point
During _________ Acid-Base Catalysis, water acts directly as the acid and base group.
11.
1 point
_________ catalysis uses an active site residue R group to form a covalent bond.
12.
1 point
The _________ is the site of catalysis.
13.
1 point
__________ catalysis stabilizes/shields negative charges in substrates to make a better leaving group.
14.
1 point
Enzymes lower the activation energy.
15.
1 point
Enzymes and binding proteins have specificity with respect to chiral centers.
16.
1 point
________ formation helps to orient the substrate.
17.
1 point
ATP-dependent enzymes often employ ____________.
18.
1 point
This type of catalysis occurs when a proton is transferred during the transition state.
19.
1 point
The highest energy level results in the most unstable substrate configuration.
20.
1 point
The ___________ model uses a conformational change that repositions amino acids in the active site.
21.
1 point
______________ are compounds that resemble substrates in the transition state and are potent inhibitors of enzymes.
22.
1 point
One reactant is not energetically favored over two.
23.
1 point
Alignment of reactive chemical groups is critical for all enzymes.
24.
1 point
___________ are typically proteins that act as a biological catalyst thus increasing the rate of a reaction.
25.
1 point
RNase has 2 histidine residues that function in acid-base.
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