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MTC 1 > Week 5- Enzymes > Flashcards

Week 5- Enzymes Flashcards

1
Q

catabolic pathways?

A 
breaking down (glucose broken down for energy)
requires energy
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2
Q

anabolic pathways?

A 
synthetic pathways (synthesis of glucose from amino acids)
requires energy
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3
Q

what is exergonic?

A

reactions release free energy
reactants are like a ball rolling down a hill
catabolism, generates disorder
delta G <0, spontaneous reaction

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4
Q

what is endergonic?

A

reactions consume free energy
reactants are like a ball going up a hill
anabolism, order increases
delta G >0, non-spontaneous reaction

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5
Q

how is activation energy reduced?

A

enzymes (catalyst)

final equilibrium and delta G don’t change

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6
Q

what are the 3 basic steps of enzyme catalysts?

A

1- binding of substrate
2- conversion of bound substrate to bound product
3- release of product

done in the active site of the enzyme

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7
Q

how do enzymes work?

A
  • they have a specific active site that binds the substrate
  • can change the shape of the substrate to facilitate product formation
  • bind cofactors (coenzymes that also facilitate substrate change) can be metal ions or organic molecules
  • stretch bonds in substrate molecules, making them unstable and more reactive to the action of other substrates
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8
Q

what is acid-base catalysis?

A

enzyme side chains transfer H+ to or from the substrate causing a covalent bond break

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9
Q

what is covalent catalysis?

A

a functional group in a side chain bonds covalently with the substrate

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10
Q

what is metal ion catalysis?

A

metals on side chains loose or gain electrons

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11
Q

first law of thermodynamics?

A

in energy conversion the total energy remains constant (enthalpy)
no energy is created or lost in conversion

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12
Q

second law of thermodynamics?

A

universe tends towards disorder (entropy)

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13
Q

which way is the reaction going to shift with a negative delta G?

A

right (forward)

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14
Q

which way is the reaction going to shift with a positive delta G?

A

left (reverse)

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15
Q

what does delta G do?

A
  • mechanical work (muscles)
  • transport work (carrier proteins)
  • biochemical work (makes molecules)
  • thermogenesis (ATP oxidation, heat)
  • energy from fuel oxidation (NADH, FADH)
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16
Q

Apoenzymes?

A

lacking cofactors

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17
Q

Haloenzymes?

A

have cofactors

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18
Q

what functional group does NAD accept?

A

hydride ions from lactate

19
Q

what functional group does FAD accept?

A

2 electrons as 2 hydrogen atoms

20
Q

oxireductases?

A

catalyze oxidation and reduction reactions

dehydrogenases: transfer hydrogen between a substrate and a coenzyme (NAD, FAD etc)

21
Q

transferases?

kinases?

A

transfer a specific functional group from the donor molecule to the acceptor molecule

transfer phosphate from ATP to a second substrate

22
Q

hydrolases?

A

hydrolysis reaction where bonds (CO, CS, CN) are cleaved by the addition of water
eg, digestive enzymes and lysosomal enzymes

23
Q

lyases?

carboxylases?

A

cleaving bonds in another way other than hydrolysis or ox- reduction
eg, aldolase, thiolases

carbon lyases that remove or add carboxyl group from organic compounds

24
Q

isomerases?

A

can convert a molecule from one isomer to another

eg, mutase catalyzes the shifting of a functional group from one position to another within the same molecule

25
Q

ligase? (synthetases)

A 
synthesize bonds (CO, CS, CN, CC) in reactions couple to the cleavage of a high energy phosphate bond in ATP 
eg, DNA ligase
26
Q

units for Vmax?

km?

A

umol/min/mg

mM

27
Q

when do enzymes have high affinity for their substrate?

A

at low substrate concentrations

28
Q

does glucosekinase have a high or low affinity for a substrate?

A

low affinity for glucose so it requires a higher glucose concentration to function

29
Q

reversible inhibition?

competitive inhibition?

A
  • inhibitor binds non-covalently to the active site and prevents substrate from binding
  • competitive inhibition, if substrate concentration is increased than the substrate will bind to the active site
  • this increases the Km but no effect on Vmax
30
Q

uncompetitive inhibitor?

A
  • allosterically binds to the enzyme substrate complex and prevents the complex from releasing substrate
  • it cannot be surmounted
  • increasing the inhibitor will lower Vmax
31
Q

non-competive inhibitor?

A
  • binds to the enzyme allosterically, changes shape and alters the active site
  • decreases the amount of active enzyme and reduces Vmax
32
Q

irreversible inhibitor?

A

inhibitor binds covalently to the active site and permanently inactivates the enzyme

33
Q

allosteric regulation?

A

effector molecule that binds to a regulatory subunit inducing the enzyme to change its shape
- can inhibit or activate the enzyme

34
Q

allosteric enzymes?

A
  • have multiple active site

- sensitive to low concentrations of inhibitors, important in regulating the entire metabolic pathway

35
Q

non- allosteric enzymes?

A
  • have one active site

- small changes in activator concentration can promote large changes in the reaction

36
Q

what are isozymes?

A
  • different form of the same enzyme
  • catalyze the same reaction but have different properties (temperature)
  • organisms can use to adjust temperature changes
37
Q

what happens to enzymes at high temperature?

A

non-covalent bonds break, loose its tertiary structure and is denatured

38
Q

what enzymes measure liver damage?

and for cardiac damage?

A

aspartate and alanine aminotransferases

creatinine kinase

39
Q

Beers Law?

A

the amount of light absorbed by a compound in a solution is directly related to the concentration of the compound in solution

40
Q

activation transfer coenzymes?

A

participate in catalysis by binding with a substrate

41
Q

oxidation reduction coenzymes?

A

do not form covalent bonds with the substrate

42
Q

cystic fibrosis?

A

Cl- secretion and secretion of water and other ions is impaired
this alters the pH and dehydrates secretions that participate and obstruct the lumen = causing inflammation and degradation of the pancreas, liver, gall bladder, intestine.

43
Q

pancreatitis?

A

inflammation of the pancreas

caused by high levels of amylase (break down starch) and lipase (digest fats) in the blood stream

MTC 1 (4 decks)

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