Enzymes Flashcards

1
Q

Enzymes

A

Protein catalysts that inc. rate of rxn w/o being changed

  • direct all metabolic events
  • don’t invent new rxns
  • life not possible w/o them
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2
Q

Enzyme nomenclature

A
  1. Oxidorectuctases
  2. Transferases
  3. Hydro leases
  4. Leases
  5. Isomerases
  6. Ligases
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3
Q

Oxidoreductases

A

Redox rxns

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4
Q

Transferases

A

Transfer C, N, and P containing groups

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5
Q

Hydrolases

A

Cleave bonds w/ H2O

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6
Q

Lyases

A

Cleave C-C, C-S, and C-N

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7
Q

Isomerases

A

Rearrangement of optic or geometric isomers

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8
Q

Ligases

A

Creates carbon bonds w/ O, S, and N

  • coupled w/ hydrolysis of ATP (GTP)
  • endergonic
  • opposite of ligase
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9
Q

Synthase vs. synthetase

A
  1. Synthase- no ATP

2. Synthetase- required ATP

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10
Q

Oxidase vs oxygenase

A
  1. Oxidase- uses O2 as acceptor w/o incorporating it

2. Oxygenase- one/both O2 atoms incorporated

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11
Q

Phosphotase vs. phosphorylase

A
  1. Phosphotase- H2O to cleanse phospho groups (hydrolases)

2. Phosphorylase- uses Pi to cleave and generate phosphorylated product

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12
Q

Enzyme structure

A
  1. Protein component
  2. Non protein components
    * cofactors- inorganic (Zn2+, Mg2+, Fe3+, Fe2+)
    * coenzymes- organic
    • vitamin derivatives: NAD+, FAD, NADP+, CoQ, CoA
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13
Q

Haloenzymes

A

Enzyme + non protein = active

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14
Q

Apoenzymes

A

Enzyme alone = inactive

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15
Q

Enzyme function

A
  • efficient
  • Specific
  • energy required
  • active site- induced fit model
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16
Q

Factors affecting Rxn Velocity

A
  1. Temp
  2. PH
  3. Substrate concentration
17
Q

Michaelis-Menten Kinetics

A

Assumptions

  1. [S]»>[E]
  2. [ES] in steady state
  3. No appreciable back rxn
    * Km= [S] needed for 1/2 Vmax
18
Q

Enzyme regulation

A
  1. Substrate available
  2. Post-translational modifications
  3. Enzyme protein production
  4. Reg. In specific environment
  5. Enzyme compartmentalizations
  6. Allosteric effectors
19
Q

Enzyme Inhibition

A
  1. Irreversible- bind w/ covalent bonds (lead poisoning)
  2. Reversible- noncovalent bonds
    * Noncompetitive- allosteric site (allopurinol)
    * competitive- active site (statin drugs)
20
Q

Competitive inhibition kinetics

A
  • Vmax = same
  • Km inc.
  • steeper line, same y-axis
21
Q

Noncompetitive Kinetics

A
  • Dec. Vmax
  • Km =
  • steeper line, same x-axis
22
Q

Allosteric effectors

A
  • Alter affinity for substrate => affect Km
  • Alter Vmax
    1. Homotropic- substrate is effector
    2. Heterotropic- effector is different molecule
  • feedback regualation
  • kinetics
  • activator: dec. Km
  • inhibitor: dec. Vmax, inc. Km