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LQB180 > Week 10 Catalysts Enzymes > Flashcards

Week 10 Catalysts Enzymes Flashcards

1
Q

Seven Basic Types of Enzymes

A

Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases
Translocases

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2
Q

Oxidoreductases

A

Catalyse oxidation reduction reactions

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3
Q

Transferases

A

Transfer functional groups

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4
Q

Hydrolases

A

Hydrolysis Reaction

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5
Q

Lyases

A

Removal of functional groups (not hydrolysis)

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6
Q

Isomerases

A

Catalyse structural reorganisation

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7
Q

Ligases

A

Molecular coupling driven by ATP (or other pyrophosphate) bonds

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8
Q

Translocases

A

Assists in moving a molecule across membrane

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9
Q

Enzyme General Properties

A
  • may contain cofactors (Metal ions, nucleotides, heme groups, vitamins etc.)
  • Enzyme structure determines function
  • Catalytically potent - thousands or millions fold faster
  • highly specific for a given reaction
  • Have defined pH and Temperature optimums
  • Kinetics: More enzyme = faster rate, more substrate = faster rate (Both situations show saturation)
  • Enzymes can be inhibited
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10
Q

Enzyme Primary Structure

A

The sequence of amino acids making the protein

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11
Q

Enzyme Secondary Structure

A

Alpha helixes, Beta sheets and coils. Motifs are defined by hydrogen bonding patterns.

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12
Q

Enzyme Tertiary Structure

A

How motifs hold together to form a polypeptide chain. Multiple secondary structure elements come together to form a single-folded polypeptide chain. Changes in direction at the molecular surface can form loops

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13
Q

Enzyme Quaternary Structure

A

How Polypeptides fit together to form an oligomeric protein. Multiple polypeptide chains assembled to form an oligomeric protein . No covalent interactions.

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14
Q

How do enzymes lower activation energy

A

Bind and stabilise substrate in the transition state

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15
Q

Fischer Lock & Key

A

Enzyme fitting into active site like a key in a lock

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16
Q

Induced Fit

A

Enzyme changes shape to accommodate the substrate

17
Q

Vmax

A

Theoretical maximum velocity

18
Q

Ka

A

Disassociation constant
low - weak acid
high - strong acid

19
Q

Competitive enzyme inhibition

A

the inhibitor binds and blocks the same pocket. Reduces enzyme availability. Km up Vmax unchanged

20
Q

Noncompetitive inhibition

A

The inhibitor binds somewhere other than the active site. Reduces affinity and activity of the enzyme. V max down, Km unchanged

LQB180 (12 decks)

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