Enzymes Flashcards

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1
Q

What are globular proteins?

A

Polypeptide chains folded into a compact shape like a ball with an irregular surface
Complex tertiary and quaternary structure

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2
Q

What are fibrous proteins?

A

Individual molecules that span a large distance
Simple 3D structure

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3
Q

What is an enzyme?

A

A globular biological catalyst that speeds up metabolic reactions without being changed in the process

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4
Q

What are enzymes needed for?

A

Metabolism, movement, digestion, cell signalling and gene expression

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5
Q

What is a kinase enzyme?

A

These add phosphate ions to molecules

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6
Q

How are enzymes involved in disease?

A

May disrupt homeostasis e.g. PKU - rare genetic disorder caused by mutation leading to seizures and behavioural problems

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7
Q

What is the active site?

A

It is a cleft on the protein
It is non polar
Has specific amino acids that allow substrate to bind and others for catalysis

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8
Q

What is the induced fit model?

A

when substrates bind to the enzyme active site it will change its shape slightly so the chemical reaction can occur with the lowest energy possible

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9
Q

What is the allosteric site?

A

Away from the active site and is where regulatory molecules bind which can activate or inhibit a molecule

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10
Q

What is a co-factor?

A

Any inorganic factor required for enzyme activity e.g. metal ions for metalloenzymes

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11
Q

What is a coenzyme?

A

An organic molecule that is directly involved in enzyme catalysis e.g. lactate dehydrogenase

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12
Q

What is an apoenzyme?

A

Inactive - no coenzyme added

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13
Q

What is a holoenzyme?

A

Active - coenzyme added

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14
Q

What is a prosthetic group?

A

Non protein molecules that are associated with the enzyme via covalent bonds

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15
Q

What do oxidoreductases do?

A

Transfer oxygen or hydrogen atoms or electrons from one substrate to another

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16
Q

What do transferases do?

A

Transfer a functional group form one substrate to another

17
Q

What do hydrolases do?

A

Hydrolysis of substrate

18
Q

What do lyases do?

A

Addition or removal of a group to form a double bond

19
Q

What do isomerases do ?

A

Transfer of groups within a molecule

20
Q

What do ligases do?

A

Bond formation coupled with ATP hydrolysis

21
Q

What is activation energy?

A

Amount of energy needed to start a reaction

22
Q

What is the transition state?

A

Highest energy level as the substrate is in the process of being converted to products (most unstable)

23
Q

What are 7 ways enzymes reduce activation energy?

A

Binding(collision theory) - substrates need to collide with each other with enough energy
Spatial complementarity- reactants in the right orientation
Induced fit- a.s. adjusts shape so substrate bound in best way
Chemical complementarity- specific a/a allow catalysis
Specific r groups - define shape of a.s
Exclude water
Weak forces- release enery

24
Q

What are the catalytic mechanisms?

A

Metal ion catalysis - metal ion aids catalysis
Catalysis by approximation- brings reactants closer together
Covalent catalysis- enzyme uses a transient bond to bind the substrate
Acid base catalysis- Hydrogen added or taken away for reaction to occur

25
Q

What is the RoR / velocity ?

A

Amount of substrate converted to products per unit time

26
Q

Outline the initial velocity

A

Units are µmol/min
Fastest rate, high concn of substrate, low products, low feedback inhibition

27
Q

What is the Michaelis constant?

A

Measure of affinity of the substrate to the enzyme- how readily the substrate binds to enzyme

28
Q

How to calculate Km

A
  1. Vmax line to Y axis
  2. Half of Vmax line - line down to the x axis
  3. Km- concn of substrate when Vmax is at its half point
29
Q

What does a high Km mean?

A

Weak binding
Low affinity
High concn of substrate to reach Vmax

30
Q

What is the effect of temperature on RoR?

A

Increase in thermal energy so overcomes the Ae which increases rate
BUT beyond optimal
Rapid decrease in RoR as weak bonds broken altering active site
enzyme denatured

31
Q

How does pH impact enzyme activity?

A

Ionisation of groups in the active site

32
Q

How are enzymes regulated?

A
  • Controls how molecules of each enzyme it makes by regulating the expression of the gene that encodes that enzyme
  • Confining sets of enzymes to particular subcellular compartments
  • Covalently modified to control activity
  • Rate of protein destruction
  • Binding of small molecules
33
Q

What is feedback regulation?

A

End products inhibit earlier pathway steps to prevent the build up of unnecessary metabolites

34
Q

What is competitive inhibition?

A

Inhibitor is a similar shape to the substrate so it binds to the active site of the, blocking the binding of substrates. Can be overcome by increasing substrate concn
Km increases
Affinity decreases
Vmax same

35
Q

What is non competitive inhibitors?

A

Inhibitor binds to the allosteric site causing conformational changes to the active site the binding of the substrate is the same BUT catalytic activity is decreased
Km is the same
Vmax is reduced

36
Q

What is an uncompetitive inhibitor?

A

An inhibitor binds to the e.s complex thus inhibiting catalysis
Km is reduced
Vmax is reduced