Energy and Enzymes Flashcards

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1
Q

metabolism

A

sum of all chemical reactions in one organism

extract energy from nutrients

synthesize or breakdown molecules

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2
Q

catabolism

A

reactions that release energy by breaking down molecules (exergonic)

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3
Q

anabolism

A

reactions that require energy to build molecules *endergonic

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4
Q

energy

A

capacity to do work

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5
Q

chemical work

A

making and breaking chemical bonds, building and breaking molecules

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6
Q

kinetic work

A

move ion, molecules, large stuff in and out of the cell, move a cell through a tissue of the body

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7
Q

kinetic energy

A

energy of motion

ex: moving Na+ across the membrane down its concentration gradient
rolling a ball down a hill

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8
Q

potential energy

A

stored energy aka energy that’s about to happen

ex: ball poised at the top of the hill
disequilibrium of Na+ ready to move down its concentration gradient

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9
Q

thermal energy

A

heat

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10
Q

chemical energy

A

potential energy in food or storage molecules

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11
Q

energy transformations

A

constant changes of energy from one form to another

potential energy–>kinetic energy
chemical energy –>thermal energy

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12
Q

thermodynamics

A

study of energy transformations

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13
Q

1st law

A

energy can be neither created nor destroyed just converted from one form to another

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14
Q

2nd law

A

every energy transfer or transformation increases entropy

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15
Q

entropy

A

energy lost when trying to convert from one form to another

results in unusable energy

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16
Q

intermediates

A

molecules involved in reactions that have many steps

A+B–>C–>D–>E

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17
Q

exergonic reaction

A

when you break a bond, energy is released

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18
Q

endergonic reaction

A

when you make a new bond, energy is required

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19
Q

where do we get energy for endergonic reactions?

A

o we can couple an endergonic and exergonic reaction at the same place/time. Use energy from one to fuel the other
o we can store energy as potential energy in electrons carried on nucleotides (NADH, FADH2)
o These energy transfer molecules carry the energy until it can be used in the ADP-ATP conversion
o Side note: ATP forms the bridge between endergonic and exergonic reactions

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20
Q

Cellular reactions

A

• Often reversible
o Often different enzymes are required for each direction-another level of control!
o Either catabolic or anabolic
o A+b←→C +D

21
Q

activation energy

A

energy needed to start a reaction

energy required to bring two molecules close together

22
Q

enzymes

A

proteins that catalyze or speed up reactions

23
Q

substrate

A

ligand

molecule that the enzyme acts on

24
Q

co-factor

A

another binding partner that may control the enzyme

enzymes get too powerful so in order to maintain homeostasis so we need a co-factor to control enzyme activity

keep enzyme inactive, activate when needed

25
Q

active site

A

grooves or pockets in the 3-D protein where enzymes bind their substrates

made up of amino acids

26
Q

enzyme-substrate complex

A

a temporary molecule including the enzyme and substrates

27
Q

steps to catalyze a reaction

A

o Enzyme binds substrate forms enzyme-substrate complex
• A temporary molecule including the enzyme and substrates
o Chemical reaction occurs—enzyme is not bound to product
o Enzyme releases product
• E+S→ES→EP→E+P
• Lactase and lactose form a lactose-lactase complex, then forms an enzyme product complex, then it will release them back into their monomers
o While enzyme is bound, it cannot produce more substrate

28
Q

enzyme function

A
  • Each enzyme molecule has a single active site
  • Once a substrate molecule is bound, the active site is “taken” temporarily
  • At the end of the reaction, the products are released and the enzyme is ready to bind to a new substrate
29
Q

turnover number

A

number of molecules of substrate that the enzyme can process per second

all enzymes have it

30
Q

turnover number is determined by its

A

affinity

31
Q

affinity

A

strength that a protein has towards its ligand

enzyme has towards its substrate

32
Q

more molecules will be passed if your affinity is

A

LOWER

33
Q

binding

A

occurs when a set of noncovalent interactions tie the proteins together

34
Q

affinity proteins

A

hemoglobin
can bind CO2, H+, and CO
has a stronger affinity for CO than O2

35
Q

if affinity is stronger

A

turnover rate decreases

36
Q

an active site will demonstrate more specificity and a higher affinity for its ligand when

A

the site of interaction is more complex

37
Q

inhibitor

A

if an inhibitor has a higher affinity for the enzyme than the substrate, there will be a powerful inhibition

38
Q

affinity of the enzyme for its substrate determines

A

turnover number

39
Q

saturation

A

what happens when an enzyme is operating at its turnover number

reached when each molecule is bound to a substrate and you cannot increase the rate of reaction

40
Q

competitive inhibitor

A

something that binds to a substrate’s active site

both molecules are competing for that active site

41
Q

allosteric inhibitor

A

binds to a separate site enzyme, which changes the shape of the substrate active site so substrate can no longer bind

low affinity

42
Q

competitive inhibition

A

both the inhibitor and the substrate bind to the same active site

due to turnover number, this reduces enzyme activity

if binding of inhibitor has higher affinity than substrate, this can eliminate enzyme activity

43
Q

beta blockers

A
  • Binds to the epinephrine receptor and blocks it
  • Has a higher affinity than epinephrine
  • Reduces the rate at which our cells can bind to epinephrine
  • Effects: lowers heart rate
  • Nervous effects don’t happen
  • Tamoxifen
44
Q

feedback inhibition

A

product of the pathway acts as an inhibitor to the first steps of the pathway

ex: • Highlevel of testosterone, it inhibits the first enzyme, leads to fewer testosterone molecules being produced
• When we fall short with testosterone, it unhibits and then the regular amount of testosterone will continue to be produced

45
Q

phosphorylation

A

addition of a phosphate group

46
Q

kinases

A

enzymes that add phosphate groups

47
Q

phosphatases

A

enzymes that remove phosphate groups

48
Q

lysozyme

A

o Cuts polysaccharide chains on bacterial cell walls by hydrolysis
o These chains are relatively stable until lysozyme binds and bends the substrate, altering the molecular shape and making it vulnerable to water