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BMS1011 > ENZYME ACTIONS > Flashcards

ENZYME ACTIONS Flashcards

1
Q

What are the reactant conditions for enzymes in biological systems?

A

37 degrees celcius (low temps), Low reactant concentrations, neutral pH (except for stomach and lysosomes)

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2
Q

Which enzyme is very general and can break any peptide bond?

A

chymotripsin

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3
Q

What do isomerases do?

A

Change arangement of functional groups

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4
Q

What do lysases do?

A

Cleavage of C-C,C-O, C-N or other bonds by elimination, leaving doulbe bonds or rings, or addition of groups to double bonds.

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5
Q

What do oxidoreductases do?

A

Transfer electrons (hydride ions or H atoms)

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6
Q

What do ligases do?

A

The opposite of lysases. So they form the C-X bonds by condensation reactions.

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7
Q

Is the transition state stable or unstable?

A

UNSTABLE!! It is the state where neither original or final molecules are present.

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8
Q

Which type of binding occurs between substrate and active site?

A

NON covalent interactions; ionic bonds, H bonding, hydrophobic interactions

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9
Q

What does NOT CHANGE due to presence of enzymes?

A

Gibbs free energy or equilibrium

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10
Q

What are enzymes most adapted to binding?

A

The transition state between substrate and product, which facillitates the formation of transition state (decreasing the activation energy of the reaction)

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11
Q

What are prosthetic groups also known as?

A

Vitamins

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12
Q

What is an apo enzyme?

A

An inactive enzyme

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13
Q

What are the three types of reversible inhibition?

A

Competitive, uncompetitive, noncompetitive (mixed)

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14
Q

What is competitive inhibition?

A

Inhibitor binds to active site but is not processed

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15
Q

What is uncompetitive inhibition?

A

Inhibitor binds to separate site, inhibitor only binds to ES complex not just the enzyme.

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16
Q

What is mixed, non competitive inhibition?

A
  • inhibitor binds to a site other than the active site, may bind to E or ES complex, may not affect the binding of the substrate.
17
Q

How is the rate of enzyme catalysis measured?

A

Through:

  1. substrate dissappearance
  2. Product formation
18
Q

What is Vmax?

A

Maximal velocity that enzyme can go to at particular temp and concentration (enzyme)

19
Q

Is the michaelis mentum plot linear or curved?

A

Curved - Michaelis constant is Km.

20
Q

What is a lineweaver burke plot and what is it used for?

A

Linear plot that is the inverse of Km and Vmax and substrate concentration. (1/[s]) (1/vmax) 1/km) slope= km/vmax

  • Can see what happens to enzymes activity in the presence of an INHIBITOR.
21
Q

What are the features of the lineweaver burke plot in competitive inhibition?

A

No change in vmax, because at high sub conc. vmax will be reached. Will have AN INCREASE IN APPARENT KM. –> because efficiency of enztme interaction with substrate decreased .

22
Q

What are the features of the linweaver burke plot for uncompetitive inhibition?

A

Vmax decreases with INCREASED inhibitor (catalysis is being prevented)
- Km decreases (because locking the ES complex together)

23
Q

What are the features of the lineweaver burke plot in noncopetitive (MIXED) inhibition?

A

Vmax also dereases with INCREASED inhibitor(catalysis being prevented)
Effects on Km are combinationof INTERFERENCE BY INHIBITOR AND LOCKING OF e-S COMPLEX
mixed effect

(inhibitor can bind just with the enzme (not substrate aswell)) and ALSO bind with substrate.

24
Q

What are allosteric enzymes?

A

Have quaternweery structure. Kinetics different from Michaelis mentum.

  • BAsed on sigmoidal kinetics
  • substrate or molecular bonding induces conformational change to facilitate binding - enzyme is flexible.
25
Q

What is an exmple of a protein sharing the same properties as an allosteric enzyme?

A

Haemoglobin (T and R states)

26
Q

What are izowenzymes?

A

Enzymes that catalyse the same reaction but have different primary strucutres. (different genes produce slightly different versions) - have different primary strucutres.

27
Q

What are examples of iso-enzymes?

A

Glucokinase (12) and Hexokinase (Km 0.04) - so hexokinase is much better enzyme for reaction one of glycolysis.

28
Q

What is creatine kinase used for? (CK)

A

Clinical diagnosis in skeletal muscle, heart and brain

29
Q

What is Aspartate amino transferase used for in clinical diagnosis?

A

Heart skeletal muscles, liver ,brain

30
Q

What is lactate dehydrogenase used for in clinical diagnosis?

A

pyruvate–> lactate
LDH1: heart (mycardial infarction)
LDH5: Liver (hepatitis)

BMS1011 (5 decks)

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