week 2 - lectures 3,4 Flashcards

(49 cards)

1
Q

describe competitive inhibition

A
  • inhibitor mimics substrate and binds to active site
  • Vmax is the same
  • overcome by increasing substrate concentration
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2
Q

describe non competitive inhibition

A
  • allosteric inhibition
  • inhibitor binds to allosteric site
  • inhibitor is structurally different from substrate
  • change in enzyme conformation
  • reduced ability to form product and sometimes to bind substrate
  • Vmax is lowered
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3
Q

describe feedback inhibition and give an ex

A

non competitive inhibition
ex: citrate inhibits PFK in glycolysis

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4
Q

describe postive feedback

A

when a product activates an enzyme upstream of the metabolic pathway to continue producing this product in greater amounts

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5
Q

describe allosteric enzymes and give an ex

A

not an MM enzyme
multiple subunits/polypeptides/active sites per enzyme - quaternary structure
exists in active and inactive forms
substrate binding is cooperative (one substrate binding helps the other too)
ex: phosphofructokinase (PFK)

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6
Q

describe irreversible inhibition and give an ex

A

chemical capable of reacting covalently with amino acid residues at active site or elsewhere - destroys enzyme
also can occur if non covalent binding is so strong that it is irreversible
ex= penicillin inhibits formation of bacteria cell wall

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7
Q

what type of reaction is cellular respiration

A

redox reaction

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8
Q

describe redox reactions

A

catabolic, exergonic
electron donor is oxidized and electron acceptor is reduced
electrons lose energy and become lower energy electrons

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9
Q

describe the components of a redox reaction

A

reducing agent (e- donor)
oxidizing agent (e- acceptor)
oxidized form (“e- donor”)
reduced form (low energy e-, e- acceptor)

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10
Q

state overall cellular respiration equation

A

drop in free energy from glucose —> G3P —> pyruvate —> acetylcoA —> CO2

C6H12O6 + 6O2 —> 6CO2 + 6 H2O + energy

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11
Q

describe cellular respiration equation

A

glucose = high energy electrons, reducing agent
oxygen = electron acceptor, strong oxidizing agent

glucose to CO2 (oxidized) = oxidation
oxygen to water (reduced, low energy electron acceptor) = reduction

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12
Q

how many electrons transferred during CR

A

24

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13
Q

how many atps produced from cr

A

30-32 atps

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14
Q

describe the exergonic aspect of cr

A

ΔG<0
ΔG* = -686kcal/mol glucose
ΔG* = 7.3kcal/mol atp synthesized
much energy lost by heat (should make 93 atps but only makes 30-32), approx 60% energy converted to heat

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15
Q

describe first step of cellular respiration

A

10 steps linear
complete oxidation of glucose by aerobic respiration
occurs in cytoplasm
converts glucose (6C) to 2 pyruvates (2x3C)

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16
Q

describe step 2 of cellular respiration

A

acetyl coa formation = pyruvate oxidation
occurs in matrix of mitochondria
oxidative decarboxylation of pyruvate (3C) to form acetyl coa (2C) x2

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17
Q

state net production of acetyl coa formation

A

2 NADH and 2CO2 (per glucose)

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18
Q

state net production of glycolysis

A

net production of 2 atp by substrate level phosphorylation (slp) and 2 NADH (per glucose)

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19
Q

what is step 3 of cellular respiration

A

8 steps circular
citric acid / kreb cycle
multi step reactions
occur in matrix
complete oxidative decarboxylation of acetyl coa

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20
Q

state net production of citric acid cycle

A

6 NADH and 2 FADH2 and 4CO2 per glucose, 2 GTP (atp) by slp

21
Q

after what step is glucose completely oxidized to 6CO2

A

step 3
citric acid cycle
all electrons are carried by 10 NADH and 2FADH2

22
Q

describe step 4 of cellular respiration

A

oxidative phosphorylation
has 2 steps
exergonic and endergonic processes are coupled

23
Q

describe first step of oxidative phosphorylation

A

electron transport train (ETC)
inner membrane of mitochondria, FADH2—> O2
the electrons move from NADH through complexes to oxygen
electrons lose free energy (exergonic)
energy released creates a proton gradient (endergonic)

24
Q

describe second step of oxidative phosphorylation

A

chemiosmosis
diffusion of protons down their electromagnetic gradient is couple to atp synthesis by atp synthase located in inner membrane of mitochondria
proton diffusion = exergonic
atp synthesis = endergonic

25
what is net synthesis of chemiosmosis
26-28 atp per glucose
26
describe atp synthase
molecular mill multiple subunits (rotor) quaternary structure atp is synthesized from adp and inorganic phosphate Pi
27
describe energy transformations of atp synthase
electrochemical potential energy of the proton gradient —> kinetic energy (turning of rotor) —> chemical energy (bond formation in synthesis of atp)
28
name the 3 enzymes involved with cellular respiration
kinase dehydrogenase - oxireductase isomerase
29
describe kinase
transfers a phosphate onto an OH group of a molecule kinase = transferase (functional group of molecule is transferred to another) slp (substrate-p + adp —> product + atp catalysed by kinase overall exergonic
30
describe dehydrogenase-oxireductase
catalyses redox reactions by transferring electrons NAD+ and FAD are oxidizing agents (accept electrons), become reduced to NADH & FADH2, each carry 2 high energy electrons
31
describe isomerase (ex)
ketose sugar converted to aldose by isomerase
32
describe step 3 of glycolysis and the types of inhibition/activation
- first real committed step of glycolysis - phosphofructokinase - allosteric enzyme - pfk is inhibited by high levels of atp (allosteric enzyme) - pfk is stimulated by high levels of AMP-ADP (allosteric activation) - pfk is inhibited by high levels of citrate which accumulates if krebs cycle functions too slow relative to glycolysis (feedback inhibition, negative feedback)
33
name the two situations of fate of pyruvate
aerobic conditions = converted to acetyl coa and enters kreb cycle anaerobic conditions = fermentation
34
describe the mitochondrial electron transport chain (carriers)
two mobile electron carriers (UQ and cytochrome (cyt c))
35
state overall redox for op (NADH)
NADH + 1/2 O2 —> NAD+ + H2O
36
describe deficiencies
vitamin b are coenzymes of important metabolic enzymes affect energy metabolism, causes fatigue, anemia, skin disorders, muscle and nervous system malfunction
37
describe alternative catabolic pathways
fatty acids, glycerol and amino acids can also be oxidized fats are hydrolyzed to glycerol and fatty acids glycerol is converted to G3P by phosphorylation fatty acids are converted to acetyl coa by beta-oxidation
38
describe fermentation under anaerobic conditions
pyruvate réduction to lactate or alcohol is coupled to oxidation of NADH goal = recycle NADH to NAD+ allowing continued synthesis of atp by glycolysis
39
what is oxidative decarboxylation (in terms of dehydrogenase-oxireductase)
release of CO2 occurs at the same time as electron transfer reactions (redox)
40
if primary electron donor is NADH give equation order (ETC)
NADH —>complex i —> UQ —> complex iii —> cyt c —> complex iv (cytochrome c oxidase) —> O2
41
if primary electron donor is FADH2 state equation order
FADH2 —> complex ii —> UQ —> complex iii —> cyt c —> complex iv —> O2
42
describe carrying capacity of FADH2
carries lower energy electrons than NADH produces less atp than NADH H+ gradient is not as steep when FADH2 is electron donor
43
when are fats oxidized
glucose is limiting fasting dieting sleeping exercising for a long time
44
explain when proteins are oxidized
only under extreme starvation or disease proteins are hydrolyzed to amino acids amino acids are deaminated and converted into intermediates of kreb cycle (pyruvate and acetyl coa)
45
what products does fermentation produce (yeast and muscles)
total of 2 atp per glucose occurs in cytoplasm 1 glucose produces - yeast = 2 CO2 + 2 ethanol + 2 atp (glycolysis) - muscle = 2 lactate + 2atp (glycolysis)
46
what happens to a cell when there is no NAD+
no glycolysis (no acetylcoa formation, no citric acid cycle), no atp = CELL DEATH
47
step 3 of glycolysis equation
fructose 6P + atp —> fructose biphosphate + adp
48
name the 3 steps that converts pyruvate into acetyl coa (fate of pyruvate, aerobic conditions
- pyruvate dehydrogenase (in matrix, allosteric enzyme) decarboxylation redox thioesther bond (unstable, makes acetyl coa more reactive
49
conversion factors of cr
cytoplasmic NADH = 1.5-2.5 atp (1.5 = FADH2) matrix FADH2 = 1.5 atp matrix NADH = 2.5 atp