Chapter 8: Energy, Enzymes and Metabolism Flashcards

1
Q

energy

A

the capacity to do work, or capacity of change

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2
Q

potential energy

A

stored energy– as chemical bonds, concentration gradient, charge imbalance, etc.

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3
Q

kinetic energy

A

energy of movement

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4
Q

metabolism

A

sum total of all chemical reactions in an organism

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5
Q

anabolic reactions

A

complex molecules are made from simple molecules; energy input is required

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6
Q

catabolic reactions

A

complex molecules are broken down to simpler ones; energy is released

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7
Q

laws of thermodynamics

A

apply to all matter and all energy transformations in the universe

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8
Q

first law of thermodynamics

A

energy is neither created or destroyed, when energy is converted total energy before and after conversion is the same.

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9
Q

second law of thermodynamics

A

when energy is converted from one form to another, some energy becomes unavailable for work, no energy transformation is 100% efficient

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10
Q

entropy

A

measure of disorder in a system

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11
Q

total energy = free energy + unusable energy

A

enthalpy (H) = free energy (G) + entropy (S)

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12
Q

change of energy in a reaction

A

△G = △H - T△S

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13
Q

△G is negative

A

catabolic

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14
Q

△G is positive

A

anabolic

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15
Q

exergonic

A

reactions release free energy (-△G): Catabolism complexity decreases

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16
Q

endergonic

A

reactions consume free energy (+△G): Anabolism complexity increases

17
Q

chemical equilibrium

18
Q

catalysts

A

speed up the rate of a reactions, lower activation energy

19
Q

Activation Energy

A

amount of energy required to start a reaction

20
Q

transition state intermediates

A

activation energy changes reactants into unusable forms with higher free energy

21
Q

Enzyme Substrate Complex

A

held together by hydrogen bonds, electrical attraction, or covalent bonds
E + S ⇨ ES ⇨ E + P

22
Q

Acid Base Catalyst

A

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

23
Q

covalent catalyst

A

functional group in a side chain bond covalently with substrate

24
Q

metal ion catalysts

A

metal on side chains lose or gain electrons

25
cofactors
inorganic ions
26
coenzymes
small carbon-containing molecules; not bound permanently to enzymes, requires for action of enzyme
27
prosthetic groups
non-amino acid groups permenantly bound to enzymes
28
inhibitors
molecules that bind to enzyme and slower reactions
29
irreversible inhabitation
inhibitor covalently bonds to side chains in the active site--permanently inactivates the enzyme
30
reversible inhibition
inhibitors bonds noncovalently to active site, prevents substrate from binding
31
competitive inhibitors
complete with natural substrate for binding sites. when concentration of competitive inhibitor reduced
32
noncompetitive inhibitors
bind to the enzyme at a different site. enzyme changes shape an alters the active site
33
allosteric regulation
effector molecules binds to a regulatory subunit
34
metabolic pathways
first reactions is commitment step-- other reactions then happen in sequence
35
feedback inhibition
final product acts as a noncompetitive inhibitor of first enzyme which shuts down pathway