Enzymes Flashcards

1
Q

Give function and examples of oxidoreductases.

A
  • Move electrons

- NADH, NADPH, FADH2, FMNH

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2
Q

Give function and examples of Transferases.

A
  • Move a functional group

- ATP, SAM, Pyridoxal phosphate, 5’-deoxy…, tetrahydrofolate

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3
Q

Give function hydrolases.

A
  • Break chemical bonds via hydrolysis
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4
Q

Give function of isomerase.

A

Rearrange order of atoms in a molecule

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5
Q

Give function of lyases.

A

Break a chemical bond w/out water

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6
Q

Give function and examples of ligases .

A
  • Make chemical bond using ATP

- TPP, CoASH, Lipoamide, biotin

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7
Q

What are characteristics of an active site?

A
  1. Is only a few residues out of the protein
  2. Is a 3-D cleft/crevice/pocket, creating a unique microenvironment
  3. Determines substrate specificity by size and charge complementarity 4. Contacts with the substrate through noncovalent interactions
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8
Q

What is characteristic of allosteric binding?

A
  1. Does NOT occur at the active site, but follows the same interaction rules as an active site
  2. Involves a second substrate, which can be an activator or an inhibitor
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9
Q

Compare and contrast Apo and Holoenzymes

A

Apoenzymes:
• Incomplete
• Inactive
• Lack cofactor/coenzyme

Holoenzymes: 
• Whole 
• Active 
• Contain cofactor/coenzyme 
• Require allosteric activation!
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10
Q

What is Y and how is it calculated?? What are possible values for Y and what they mean?

A

Fractional saturation Y = [E-S]/[E]+[E-S]
= [S]/KD+[S]

Y = 0 - no ligand bound
Y = 0.5 - half saturated
Y = 1 - saturated
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11
Q

What is cooperativety?

A

Binding of each subsequent ligand influences the affinity (strength of interaction) of the next ligand to bind an active site

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12
Q

How do we interpret cooperativity?

A

In terms of cooperativity, we interpret Hill Coefficients in the following way:
• nH = 1 means nocooperativity
(sites are independent)
• nH > 1 means positivecooperativity
(affinity increases)
• 0 < nH < 1 means negativecooperativity
(affinity decreases)

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