Exam 4 Old Flashcards

1
Q

Which of these situations would result in a decrease of enzymes reaction rate?
Enzyme provides more efficient path toward product
Enzyme decreases entropy of substrate in activate site
Enzyme destabilizes transition state
Enzyme increases entropy of surroundings
Enzyme mutation causes increase in kcat

A

Enzyme destabilizes transition state

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2
Q

Which of these statements regarding critical aspects of enzyme structure and function is incorrect?
Enzymes typically bind to substrates with low specificity
Enzymes typically bind to substrates with high affinity
Enzymes undergo conformational change upon substrate binding
Enzyme function is highly regulated
Each of these statements is correct

A

Enzymes typically bind to substrates with low specificity

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3
Q

Which of the following statements is false for the reaction s->p
Enzymes increase the rate constant for the reverse reaction
Enzymes decrease the activation energy of reaction
Enzymes decrease the standard free energy change for a reaction
Enzymes do not alter equilibrium constant
Enzymes increase the rate constant for the forward reaction

A

Enzymes decrease the activation energy of reaction

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4
Q

Vitamin B1 is required for the function of the transketoloase enzyme. It is considered a

A

Coenzyme and the enzyme without B1 bound is called an Apo enzyme

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5
Q

During the chymotrypsin mechanism, ___ acts as a general acid and base while ___ acts as a nucleophile

A

Histidine; serine

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6
Q

Think of energy coordinate diagrams and the chymotrypsin mechanism. given that the tetrahedral intermediate in the chymotrypsin mechanism is equivalent to the transition state for this enzyme, which of the following statements would be false?
The tetrahedra intermediate is less stable, energetically than the substrate
The tetrahedral intermediate has lower energy than the substrate
The tetrahedral intermediate is attached to chymotrypsin with a covalent bond
Chymotrypsin has more intermolecular forces with tetrahedral intermediate then it does with the substrate
Chymotrypsin binds the tetrahedral intermediate with greater affinity than it does the substrate

A

The tetrahedral intermediate has lower energy than the substrate

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7
Q

This image shows the proposed mechanism for Covid like protease. This enzyme carries out which type of reaction

A

Both acid base and covalent catalysis

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8
Q

Let’s take a closer look at covid Papin like protease mechanism. When the substrate docks to this protease, Asp pushed closer to His, allowing His to convert Ser into a strong ___.

A

Nucleophile

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9
Q

An inhibitor that binds to both the free enzyme and the enzyme substrate complex, but with unequal affinity is known as

A

Mixed non competitive

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10
Q

A study is carried out in the absence and presence of a pure non competitive inhibitor. If the inhibitor is increase significantly during the experiment, the Vmax would ___ and the Km would ___

A

Decrease; no change

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11
Q

Given the Lineweaver-Burk equation provided below, representing an enzyme in the absence and presence of an inhibitor, we can see that this is a ___ inhibitor
Control: y= 1.37x +42
With 15 nm inhibitor: y= 1.37x + 65

A

Uncompetitive

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12
Q

If an allosteric enzyme is treated with a positive allosteric modulator, the K 1/2 will ___ and the initial velocity vs substrate concentration will shift ____

A

Decrease; left

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13
Q

Elastin is a serine protease that is first translated as a larger protein. Once cleaved, it is fully activated. Based on the information provided, this protein is

A

A zymogen/ proemzyme

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14
Q

Each of the following is a feature of signal transduction except
Altered rates of gene expression
Protein conformational changes
Covalent protein modification
Signal amplification
All of these are features

A

All of these are features

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15
Q

The hormone alpha-MSH helps to decrease appetite. This hormone is produced by th e POMC neurons in the anterior pituitary and when released form these cells, alpha-MSH binds to anotexigenic neurons also located in the anterior pituitary. In this situation alpha-MSH is acting as a ____ hormone

A

Paracrine

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16
Q

Related to the nitric oxide signaling pathway, vasodilation would be increased by

A

The decreased activity of cGMP phosphodiesterase

17
Q

For the activity of an allosteric protein in presence of negative modulator
How will proteins affinity change?
How will proteins activity change

A

Decrease
Decrease

18
Q

Regarding the ATCase
Will the proteins activity curve shift left or right?
How does the proteins affinity for substrate change in presence of ATP?
Will the protein shift to relaxed or tense state upon CTP binding
How will proteins K1/2 change upon CTP binding

A

Left
Increase affinity
Tense
Increase

19
Q

Explain which curve would represent activity of ATCase in presence of ATP

A

Has increased affinity and activity curve shifts left when ATP binds.

20
Q

Describe the role of Asp in the chymotrypsin mechanism

A

Pushes closer to His, His will have increased pKa and becomes a base

21
Q

Describe the role of His in the chymotrypsin mechanism

A

His acts as a general acid/base either accepting or donating a proton. When it acts as a base it accepts a proton from Serine or H2O. When it acts as an acid it donates proton to Serine and amino group

22
Q

Describe the role of Ser in the chymotrypsin mechanism

A

See is a nucleophile that attacks the carbonyl carbon, which is an electrophile, to form an oxyanion and tetrahedral intermediate

23
Q

Describe the importance of the substrate specificity pocket and oxyanion hole in the chymotrypsin mechanism

A

The substrate specificity pocket binds and orients the aromatic substrate in the mechanism. The oxyanion Joel is the location for the oxyanion in tetrahedral intermediates which are supported through intermolecular forces

24
Q

Regarding the activity of an allosteric protein in the presence of a positive modulator
How will proteins affinity for substrate change?
How will proteins activity change?

A

Increase
Increase

25
Q

Nitrate reductase contains two histidine residues the coordinate with a copper ion. When the ion is present in the enzyme, the ion is a

A

Cofactor and the enzyme without the copper bound is an apoenzyme

26
Q

An inhibitor that binds only to the free enzyme and not the enzyme substrate is known as

A

Competitive inhibition

27
Q

A study is carried out in the absence and presence of an uncompetitive inhibitor. If the inhibitor is increased significantly during the experiment the Vmax would ___ and the Km would ___

A

Decrease
Decrease

28
Q

Given the Lineweaver-Burk equations provided below, representing an enzyme in the absence and presence of an inhibitor, we can see that this is a___
Control: y= 1.56x + 18
With 15 nM inhibitor: y= 1.94x +18

A

Competitive