Energy and Enzymes Flashcards

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
active site
grooves or pockets in the 3-D protein where enzymes bind their substrates made up of amino acids
26
enzyme-substrate complex
a temporary molecule including the enzyme and substrates
27
steps to catalyze a reaction
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
enzyme function
* 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
turnover number
number of molecules of substrate that the enzyme can process per second all enzymes have it
30
turnover number is determined by its
affinity
31
affinity
strength that a protein has towards its ligand enzyme has towards its substrate
32
more molecules will be passed if your affinity is
LOWER
33
binding
occurs when a set of noncovalent interactions tie the proteins together
34
affinity proteins
hemoglobin can bind CO2, H+, and CO has a stronger affinity for CO than O2
35
if affinity is stronger
turnover rate decreases
36
an active site will demonstrate more specificity and a higher affinity for its ligand when
the site of interaction is more complex
37
inhibitor
if an inhibitor has a higher affinity for the enzyme than the substrate, there will be a powerful inhibition
38
affinity of the enzyme for its substrate determines
turnover number
39
saturation
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
competitive inhibitor
something that binds to a substrate's active site both molecules are competing for that active site
41
allosteric inhibitor
binds to a separate site enzyme, which changes the shape of the substrate active site so substrate can no longer bind low affinity
42
competitive inhibition
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
beta blockers
* 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
feedback inhibition
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
phosphorylation
addition of a phosphate group
46
kinases
enzymes that add phosphate groups
47
phosphatases
enzymes that remove phosphate groups
48
lysozyme
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