Principles of Enzyme Catalysis & Kinetics Flashcards

1
Q

What is Anfinsen’s Law?

A

“Thermodynamic Hypothesis”
The native structure of a small globular protein is determined only by the protein’s amino acid sequence.

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2
Q

What are the components of a general amino acid structure?

A

Alpha carbon, Hydrogen, amino group, carboxyl group, side chain

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3
Q

What is pKa in chemistry?

A

(pKa = -log10Ka)
Measures the strength of an acid. Lower value = Stronger acid

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4
Q

What is Ka in chemistry?

A

Dissociation constant

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5
Q

What is the Henderson-Hasselbach equation for?

A

Finds the pH of an acid or base from it’s conjugate base/acid

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6
Q

What is the Henderson-Hasselbach equation?

A

Weak acid –> pH = pKa + log (conjugate base/weak acid)

Weak base –> pH = pKa + log (conjugate acid/weak base)

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7
Q

What is the Michaelis Menten equation?

A

Vo = (Vmax[S])/(Km + [S])

Vo –> Initial velocity
[S] –> Substrate concentration
Vmax –> Maximum velocity
Km –> Substrate concentration at half Vmax

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8
Q

What dos the Michaelis Menten equation do?

A

Measures the affinity of an enzyme to bind to it’s substrate, aka: How fast a chemical reaction will occur

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9
Q

What are the general properties of enzymes?

A
  1. Substrate specificity
  2. Not destroyed in reaction
  3. pH and temp sensitive
  4. Decrease reaction energy needed
  5. Speed up reactions
  6. Mutations can result in disease or death
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10
Q

What are the different types of enzymes?

A
  1. Oxidoreductases –> H/O gained or lost
  2. Transferases –> Transfer of functional groups
  3. Hydrolases –> Break apart by addition of water
  4. Lyases –> Break apart without water
  5. Isomerases –> Rearrangement of atoms in a molecule
  6. Ligases –> Join two molecules
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11
Q

How do enzymes work?

A

Substrates bind to the active sites of enzymes and are converted into products before being released. They lower the energy needed to begin a chemical reaction, thereby triggering it to occur

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12
Q

What are the types of interactions that happen when a substrate binds to an enzyme’s active site?

A
  1. Hydrogen bonds
  2. Van der Waal bonds
  3. Hydrophobic effect
  4. Salt links
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13
Q

What is a cofactor?

A

Substance that binds to enzyme to activate enzyme, Increases the rate of reaction. Removes electrons/chemical groups from the substrate.
(Metal ions –> Mg2+, K+, Zn2+)

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14
Q

What is a coenzyme?

A

Organic molecule loosely bound to an enzyme that is required to carry out chemical reaction by acting as a electron carrier. Carries chemical groups between enzymes. Removes electrons from substrate and transfer them to other molecules.

(Vitamins, Biotin, Co-A, NAD+, FAD+)

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15
Q

What is a prosthetic group?

A

Tightly bound group of cofactors that bind to multiple types of enzymes
(Metal ions and organic molecules)

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16
Q

What is a apoenzyme?

A

Inactive enzyme; without the cofactor

17
Q

What is a holoenzyme?

A

Active enzyme; with the cofactor

18
Q

What factors affect the velocity of a chemical reaction?

A
  1. Substrate concentration
  2. Temp
  3. pH
19
Q

What is an Allosteric enzyme?

A

An enzyme with multiple active sites

20
Q

At what temp do enzymes begin to denature?

A

Enzymes start to denature at 50 degrees C or higher.