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Metabolism > Exam 1 > Flashcards

Exam 1 Flashcards

1
Q

What is the definition of metabolism?

A

Sum of all chemical reactions occurring in a living organism

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2
Q

What does it mean if there is no energy change in a chemical reaction?

A

Nothing happens

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3
Q

What are chemical reactions in living organisms catalyzed by?

A

Enzymes

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4
Q

What are enzymes attempting to drive the reaction towards?

A

Equilibrium

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5
Q

As enzyme catalyzed reactions proceed towards equilibrium what happens?

A

They release energy

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6
Q

What happens when a reaction is farther from equilibrium?

A

It releases more energy/the more energy it can release

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7
Q

What can the energy released in a chemical reaction be used for?

A

to do work, the remainder is unavailable

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8
Q

In our muscles what is the energy that is not captured to do work released as?

A

Heat

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9
Q

What is bioenergetics?

A

The study of the transformation of energy in living organisms

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10
Q

What 4 things can energy be used for?

A

Anabolic part of metabolism, contraction, transport process, control mechanism

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11
Q

What is the first law of thermodynamics?

A

In any physical or chemical change the total amount of energy in the universe remains constant, although the form of energy may change

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12
Q

What is the second law of thermodynamics?

A

In all natural processes the entropy of the universe increases

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13
Q

What does thermodynamics focus on?

A

The difference between initial and final states (changes delta)

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14
Q

What is entropy?

A

randomness or disorder

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15
Q

What is enthalpy (delta H)?

A

the change in energy of the reactions when turned into products

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16
Q

How is enthalpy change measured?

A

As the total heat energy change (delta H)

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17
Q

What is an exothermic reaction? What is it the negative value of?

A

When heat energy is given off in a reaction. delta H

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18
Q

What limits can an endothermic reaction take place in? What is it the positive value of?

A

Can only occur with the input of energy or take up heat from surroundings. Positive value for delta H

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19
Q

What is entropy change (delta S) a quantitative expression of?

A

The randomness or disorder in a system. Any change in the randomness of the system is the entropy change (delta S)

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20
Q

What is entropy change a measure of? What does this tell us?

A

a measure of energy dispersal. Tells us that energy wants to move from where it is concentrated to where it is dispersed or spread out

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21
Q

When does Delta S have a positive value?

A

Delta S has a positive value when the randomness increases

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22
Q

What is free energy change (delta G)?

A

The maximum energy available from a reaction or process that can be harnessed to do something useful

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23
Q

Of the total energy released in a reaction or process not all of it is available to _____

A

Do something useful

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24
Q

What are 3 useful things that can be done with bioenergentics?

A

Muscle contracting and lifting a load, moving ions across a membrane against their concentration gradient, synthesizing proteins from amino acids

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25
Q

When free energy is released delta G is _____ and is called _____

A

Negative, exergonic

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26
Q

Between an exergonic and endergonic reaction which is favored, which is spontaneous (can occur by itself), and is delta G positive or negative?

A

Exergonic: delta G -, spontaneous, favored
Endergonic: delta G +, not spontaneous, not favored

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27
Q

What do delta G, delta H, T, and delta S stand for?

A

delta G = free energy change, delta H = enthalpy change, T = absolute temp (Kelvin C+273=K), Delta S = entropy changes

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28
Q

What does delta G < 0 mean? _____ of the _____ is lower than the _____ of the _____

A

Free energy of the products is lower than the free energy of the reactants, exergonic

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29
Q

What is the formula for free energy changes?

A

Delta G = Delta H - T Delta S

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30
Q

When delta G > 0 is this reaction favored?

A

It is favored in the opposite direction even though it is endergonic

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31
Q

What does it mean when delta G = 0?

A

There is no free energy change

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32
Q

Is equilibrium static?

A

No, it is dynamic

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33
Q

What can’t we measure in regards to quantifying free energy? What can we measure?

A

We cannot measure exact values associated with an initial and final state of a reaction in terms of enthalpy, entropy, and free energy. We can measure energy changes over the course of a reaction as changes in enthalpy, entropy, and free energy.

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34
Q
  1. The farther the reaction is from equilibrium, the _____ the value of delta G (as a _______ value)
A
  1. Larger and negative
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35
Q
  1. From an energy perspective, when the reaction begins which values will be large and which will be small?
A
  1. A and B will be large, C and D will be small
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36
Q
  1. The natural logarithm and delta G will be ____ and _____ at the start of the reaction
A
  1. Large and negative
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37
Q
  1. What happens to the values of A and B and C and D as the reaction proceeds toward equilibrium? What will happen to delta G
A
  1. A and B will decrease and C and D will increase. Delta G will decrease but remain negative
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38
Q

What is the delta G naught value determined by?

A
  1. It is determined by the value for the equilibrium constant
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39
Q
  1. What does the delta G naught reflect?
A
  1. Reflects the energy generating potential for the reaction
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40
Q
  1. Why doesn’t the delta G naught value for a reaction define the actual energy change for the reaction inside a cell?
A
  1. Because it depends on the relative concentrations of reactants and products
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41
Q
  1. What do cells exploit energy from to synthesize ATP?
A
  1. Sunlight or food
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42
Q
  1. What is the base of adenine?
A
  1. Nitrogen
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43
Q
  1. What is ribose made up of?
A
  1. 5 carbon carbohydrate
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44
Q
  1. Hydrolysis of what linkages releases high amounts of energy?
A
  1. Phosphoanhydride
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45
Q
  1. When can ATP be hydrolyzed?
A
  1. At either linkage but not both at the same time
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46
Q
  1. Hydrolysis between the __ and ___ group is more common
A
  1. Beta and gamma
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47
Q
  1. What does hydrolysis of linkage between beta and gamma phosphoryl groups yield?
A
  1. ADP + Pi
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48
Q
  1. What does hydrolysis of linkage between beta and alpha phosphoryl groups yield?
A
  1. AMP + inorganic pyrophosphate
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49
Q
  1. What is catabolism?
A
  1. Degradation of large molecules into smaller molecules
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50
Q
  1. What are the 2 functions of catabolism?
A
  1. Produce raw materials for the synthesis of macromolecules (anabolism), and release energy, part of which is used to synthesize ATP
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51
Q
  1. What type of process is anabolism? What is the definition?
A
  1. Biosynthetic process, form molecules from smaller molecules
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52
Q
  1. What are 3 examples of anabolism?*****
A
  1. Cell growth and division, replace damaged molecules, create energy deposits
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53
Q
  1. Is a substance oxidized or reduced when it loses or accepts one or more electrons?
A
  1. Oxidation is losing, reduction is gaining
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54
Q
  1. Catabolic process usually involve oxidations of ________ this is known as _______
A
  1. Metabolites, dehydrogenations
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55
Q
  1. Anabolic processes usually include reductions of _________ by the addition of __ this is known as _______
A
  1. Metabolites, H, hydrogenations
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56
Q
  1. How are electron gain and loss connected in redox reactions?
A
  1. Directly connected
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57
Q
  1. When does most of the energy needed by our bodies to grow and survive arise? What does it do first, then eventually?
A
  1. When electrons on fuel molecules are transferred. First to coenzymes in dehydrogenation reaction then eventually to oxygen we breathe
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58
Q
  1. What are the 3 coenzymes?
A
  1. NAD, NADP, FAD
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59
Q
  1. What 3 main features do enzymes share?*****
A
  1. They increase reaction velocities, they have high specificity, their catalytic power is regulated
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60
Q
  1. What is the difference between a reversible and irreversible reaction? Which has a large energy change? Which is an equilibrium reaction? Which is more common?
A
  1. Irreversible only goes one way, irreversible, reversible, reversible
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61
Q
  1. What is the average rate?
A
  1. Change in the concentration of a reactant (substrate) or product divided by the time within this change is accomplished
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62
Q
  1. What does an enzyme increase in a reaction?
A
  1. Rate
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63
Q
  1. The increase in V attributable to an enzyme indicates _____
A
  1. Its catalytic power
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64
Q
  1. Free energy of activation is always _____
A
  1. Always positive
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65
Q
  1. When the value of delta G++ is higher what happens to the activation of the substrates, and what happens to the speed of the reaction?
A
  1. The harder the activation and the slower the reaction
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66
Q
  1. When enzymes bind substrate at an active site what does this expedite?
A
  1. Expedites the formation of the transition state which lowers delta G++
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67
Q
  1. Enzymes increase reaction rate without doing what?
A
  1. Without altering outcome of reactions
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68
Q
  1. What 5 factors affect rate of enzyme reactions?
A
  1. Substrate concentration, enzyme concentration, temperature, pH, ionic strength
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69
Q
  1. _____ is higher as _____ is increased
A
  1. Initial velocity, substrate
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70
Q
  1. What type of increase is a low S?
A
  1. Linear increase
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71
Q
  1. What happens with a higher S?*****
A
  1. V flattens out approaching a maximum velocity (Vmax)
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72
Q
  1. When V max is reached what does increasing S not produce?
A
  1. Will not produce an increase in the rate of reaction
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73
Q
  1. What is each enzyme molecule working as fast as it can to do?
A
  1. Converting S to P
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74
Q
  1. What is Michaelis constant?
A
  1. If you determine Vmax, divide it in half, then determine what S will produce one half Vmax, we get a concentration known as Michaelis constant (Km)
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75
Q
  1. How is Km defined?
A
  1. The substrate concentration needed to produce one half the maximal velocity of an enzyme catalyzed reaction
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76
Q
  1. What does the line weaver burk plot allow for?
A
  1. Allows for accurate determination of the kinetic parameters of an enzyme catalyzed reaction
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77
Q
  1. Pertaining to the line weaver burk plot, what are values determined from?
A
  1. Values are determined from intercepts on the horizontal and vertical exes
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78
Q
  1. When enzyme reaction follows Michaelis-Menton kinetics _____ over the range of substrate concentrations the L-B plot is _____
A
  1. Hyperbolic, linear
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79
Q
  1. Number of _____ converted to _____ by an enzyme molecule in a specified time when the enzyme is fully saturated with _____
A
  1. Substrate molecules, product, substrate
80
Q
  1. What does a turnover number show?
A
  1. Shows how fast an enzyme dispatches a reaction
81
Q
  1. What is a turnover number also referred to as?
A
  1. catalytic constant (Kcat)
82
Q
  1. Some enzymes catalyze a given reaction, but what is different? (In different _____, but the enzymes have different _____ for the substrates)
A

tissues, kinetic parameters

83
Q
  1. If an enzyme is saturated with substrate and is thus working as fast as possible, what will adding more enzyme do?
A

Increases the reaction velocity

84
Q

What is the enzyme proportional to?

A
  1. Vmax
85
Q
  1. Does changing enzyme have an influence on Km? What is it important in determining?
A
  1. No. Important in determining much a particular enzyme in a particular tissue
86
Q
  1. What happens to enzyme catalyzed reaction rate with an increased temperature?
A

It increases up to a poin

87
Q
  1. What happens when it’s heated too much?
A
  1. IT disrupts enzyme conformation and decreases activity
88
Q
  1. What temperature denatures enzymes?
A
  1. ~50 degrees Celsius
89
Q
  1. What is the Q10 effect?
A
  1. Describes the fold increase reaction rate for a 10 Celsius temp. For most biological processes, about 2
90
Q
  1. What does change in H+ cause? How does this influence the active site?
A
  1. Changes in H+ causes the addition or removal of protons from an enzyme molecule which may alter information. May directly influence active site
91
Q
  1. What pH range are enzymes active in? What is optimal for mammals?
A
  1. Narrow range, ~7
92
Q
  1. What may change in pH also alter?
A
  1. May alter the substrate for the enzyme, could influence rate
93
Q
  1. Ions interacting with proteins could alter what?
A
  1. Tertiary and quaternary structures
94
Q
  1. What happens to enzymes when ionic strength is too high or too low?
A
  1. Many enzymes are denatured
95
Q
  1. The activity of a variety of enzymes in the cell may be modified so that _________ is appropriate
A
  1. Cellular metabolism
96
Q
  1. Simple enzymes obeying simple _____ kinetics are common but rarely observed in _____ metabolism
A
  1. Michaelis-Menten, controlling
97
Q
  1. What are two types of regulation of enzyme activity?
A
  1. Allosteric enzymes, covalent modification of enzymes
98
Q
  1. What does activity of allosteric enzymes depend on?
    1. What is this usually comprised of?
    2. This is typically at points in metabolic pathways where ______
A
  1. S and P and the presence of positive or negative effectors
    1. Multiple subunits with multiple active sites
    2. They control overall pathway rate
99
Q
  1. Postive allosteric effectors = and negative allosteric effectors =
A
  1. Postive = activators, negative = inhibitors
100
Q
  1. Activator and inhibitors can be _____ or _____ of allosteric enzyme or other _____
A
  1. Substrate or products or other molecules (ligands)
101
Q
  1. What does concentration provide a message about?
A
  1. How active the allosteric enzyme should be
102
Q
  1. Effectors can bind to either _____ or _____ on enzyme
A
  1. Active site or allosteric sites
103
Q
  1. Activity of some enzymes can be rapidly turn on or off by what?
A
  1. Covalent modification of specific amino acid residues in the enzyme
104
Q
  1. What can an addition of a phosphate group do?
A
  1. Drastically alter a protein (reversible)
105
Q
  1. Phosphate is _____ and has _____
A
  1. Very large, 2 negative charges
106
Q
  1. What is an example of carbs being external protection for some cells?
A
  1. Cellulose
107
Q
  1. What can carbs help cells recognize?
A
  1. Molecules or other cells in environment
108
Q
  1. Carbs are part of a building block for what?
A
  1. Nucleic acids
109
Q
  1. How many carbon atoms are in tetrose, hexose, pentose, heptose, and triose?
A
  1. Tetrose = 4, hexose = 6, pentose = 5, heptose = 7, triose = 3
110
Q
  1. _____ and _____ are the smallest monosaccharides
A
  1. Glyceraldehyde and dihydroxyacetone
111
Q
  1. Both are isometric but the carbonyl groups are _____
A
  1. in different positions
112
Q
  1. What is the carbonyl group at end of carbon chain?
A
  1. Aldose
113
Q
  1. What is the carbonyl at any other position?
A
  1. Ketose
114
Q
  1. What is an example of a pentose?
A
  1. Ribose (C5H10O5)
115
Q
  1. What two formations can a pentose have?
A
  1. Open chain or cyclic formation
116
Q
  1. Cyclic form is predominant in what?
A
  1. In biological fluids
117
Q
  1. What is a five member ring with one O and four C?
A
  1. Furanose (ribofuranose)
118
Q
  1. What are the two possible isomers?
A
  1. Alpha and beta
119
Q
  1. What are 2 examples of a hexose?
A
  1. Glucose (C6H12O6) and Fructose (C6H12O6)
120
Q
  1. What is a six membered ring with one O and 5 C?
A
  1. Open chain and pyranose
121
Q
  1. What position is the carbonyl in? As opposed to?
A
  1. Position 2 in open chain, as opposed to position 1 in glucose
122
Q
  1. How many covalently linked monosaccharides are oligosaccharides?
A

2-10

123
Q
  1. What are 2 examples of a disaccharide?
A

Maltose (glucose + glucose) and Sucrose (glucose + fructose)

124
Q
  1. What is the most abundant category of carbohydrates?
A
  1. Polysaccharide
125
Q
  1. How many monosaccharide units are in a polysaccharide?
A
  1. More than 10
126
Q
  1. What are 3 examples of a polysaccharide?
A
  1. Cellulose (linear chains), starch, glycogen
127
Q
  1. Glycogen is a _____ of glucose
A
  1. Homopolysaccharide
128
Q
  1. Where is glycogen primarily found?
A
  1. Liver and muscle
129
Q
  1. What are 4 examples of lipids?
A
  1. Fatty acids, triacylglycerols, phospholipids, steroids
130
Q
  1. Fatty acids are organic acids that contain what?
A
  1. Relatively large numbers of carbons (12-26)
131
Q
  1. At physiological pH carboxyl group is _____
A
  1. Hydrophilic
132
Q
  1. Alphatic chain is _____
A
  1. Hydrophobic
133
Q
  1. Fatty acids are _____
A
  1. Amphipathic pr amphiphilic
134
Q
  1. Are fatty acids soluble in water?
A
  1. No, they are poorly soluble in water
135
Q
  1. Most fatty acids contain _____ numbers of carbon
A

Even

136
Q
  1. How are fatty acids synthesized?
A
  1. By joining acetyl groups
137
Q
  1. What do fatty acids differ in?
A
  1. Number of double bonds
138
Q
  1. What are saturated fatty acids?
A
  1. Carbons of fatty acids linked by single bonds only
139
Q
  1. What are unsaturated fatty acids?
A
  1. Double bonds between some of the carbons
140
Q
  1. What are 2 examples of unsaturated fatty acids?
A
  1. Monounsaturated, polyunsaturated
141
Q
  1. What 2 configurations can an unsaturated fatty acid have?
A
  1. Cis and trans configuration
142
Q
  1. What is the most abundant category of lipids?
A
  1. Triglycerides
143
Q
  1. What are triglycerides the main component of?
A
  1. Animal and human fat, vegetable oils
144
Q
  1. What do triglycerides serve mainly as?
A
  1. Energy depots
145
Q
  1. What 2 things do triglycerides consist of?
A
  1. Glycerol (glycerin) unit and 3 fatty acid units
146
Q
  1. Are all triaglycerols hydrophobic or hydrophilic?
A
  1. Hydrophobic
147
Q
  1. The main group of phospholipids are derivatives of _____
A
  1. Phosphatidate
148
Q
  1. What is the parent compound of all steroids and a component of the membranes of animal cells?
A
  1. Cholesterol
149
Q
  1. ATP free energy change: delta G naught for ATP is _____ and ____
A

large and negative

150
Q
  1. What is delta G naught equal to under standard conditions?
A
  1. -30.5 kJ/mol (-7.3kcal/mol)
151
Q
  1. What are concentrations of ATP, ADP, and Pi like in living cells? How does this compare to the standard 1.0 M concentrations?
A
  1. Are not identical and are much lower
152
Q
  1. The cytosol contains _____ which binds to _____ and _____
A
  1. Mg2+, ATP, ADP
153
Q
  1. In most enzyme reactions that involve ATP as a phosphoryl donor what is the true substrate?
A
  1. MgATP2-
154
Q
  1. Delta G for ATP hydrolysis in intact cells (usually denoted as delta Gp) ranges from _____ to _____
A
  1. -50 to -65 kJ/mol
155
Q
  1. Delta Gp is often called the _____
A
  1. Phosphorylation potential
156
Q
  1. What kind of a process are many cellular reactions for which ATP supplies energy NOT? What is it actually?
A
  1. NOT a simple one step process, actually a 2 step process
157
Q
  1. ATP group transfers vs simple hydrolysis: Part of the ATP molecule (phosphoryl group or adenylate moiety (AMP) is first transferred to a _____ or _____
A
  1. Substrate molecule or an amino acid residue on an enzyme
158
Q
  1. What does this covalent attachment do?
A
  1. Raises the free energy of the substrate or enzyme
159
Q
  1. What happens in the second step?
A
  1. The phosphate containing moiety is displaced generating either Pi or AMP
160
Q
  1. One important exception: those process in which non covalent binding of ATP followed by hydrolysis to ADP and Pi provide the energy to _____
A
  1. The energy to cycle a protein between two conformations producing mechanical motion
161
Q
  1. Exercise stimulates 3 of 4 processes that require ATP: _____
A
  1. Cross bridge cycle, protein movement (molecular motor), signal amplification (could be coming from 2nd messenger, intracellular mechanism, calcium induced) (4th not enhanced during exercise but pre and post exercise: anabolism)
162
Q
  1. What do these processes during exercise result in?
A
  1. Increased ATP breakdown
163
Q
  1. Catabolism is activated to do what?
A
  1. To meet the increased demand for ATP
164
Q
  1. What is accelerated during exercise?
A
  1. The entire ATD-ADP
165
Q
  1. What is ATP content of a skeletal muscle at rest?
A
  1. 6mmol/kg
166
Q
  1. As the muscle begins to contract what happens to cytosolic ATP?
A
  1. Cytosolic ATP decreases rapidly
167
Q
  1. How fast would ATP vanish during maximal contraction if sources and processes to replenish ATP were not in place?
A
  1. 3 seconds
168
Q
  1. As _____ decreases during exercise, _____ and _____ increase
A
  1. ATP, ADP, Pi
169
Q
  1. What is the formula showing that AMP increases?
A
  1. 2 ADP <> AMP + ATP
170
Q
  1. AMP? Is catalyzed by _____ or _____ because of its high level in muscle
A
  1. Adenylate kinase or myokinase
171
Q
  1. What is a synonym of AMP?
A
  1. Adenylate
172
Q
  1. What are kinases?
A
  1. Enzymes catalyzing phosphorylation of compounds using ATP (adenylate kinase named for reverse reaction in example)
173
Q
  1. How are creatine and creatine phosphate levels in muscle?
A
  1. Considerably high
174
Q
  1. What substrate is creatine even though it doesn’t make up proteins?
A
  1. Amino acid
175
Q
  1. What attachment is PCr derived from?
A
  1. The attachment of a phosphoryl group to one of creatine’s nitrogens
176
Q
  1. What is the fastest source of ATP resynthesis? When is this valuable?
A
  1. PCr, valuable during maximal exercise
177
Q
  1. What time frame does regeneration of ATP from ADP happen?
A
  1. In a single reaction
178
Q
  1. Which has a higher phosphoryl transfer potential, ATP or CP?
A
  1. CP
179
Q
  1. What is the use of PCr to regenerate ATP sometimes referred to as?
A
  1. Anaerobic alactic system
180
Q
  1. What two things does it not ___
A
  1. Does not need O2, does not generate lactate
181
Q
  1. What happens at the onset of very vigorous activity? What happens to PCr, ATP, and Cr?
A
  1. Creatine kinase (CK) drives this reaction to the right. PCr depleted, ATP maintained, Cr increases
182
Q
  1. What is the formula for phosphocreatine system?
A
  1. PCr + ADP + H+ <> CK ATP + Cr… Delta G naught = -3kcal/mol
183
Q
  1. Consumption of _____ during reaction is also _____ during high intensity exercise
A
  1. Proton, beneficial to muscle
184
Q
  1. How many genes for CK are present in mammals?
A
  1. 4
185
Q
  1. What type of cytosolic CK is found in the brain, heart, and skeletal muscle?
A
  1. CK-BB (CK1)=brain, CK-MB (CK2)=heart, CK-MM (CK3)=skeletal muscle
186
Q
  1. What sites are cytosolic isoforms located at?
A
  1. Sites where ATP is hydrolyzed and regenerated (near myosin heads, inner side of sarcolemma, outer face of SR)
187
Q
  1. Mitochondrial: involved in facilitation of _____
A
  1. Oxidative phosphorylation
188
Q
  1. CK activity can maintain _____ levels very well during intense exercise
    1. Substantial _____ effect
A
  1. ATP
    1. ATP-buffering
189
Q
  1. What kind of power for regenerating ATP does CK have?
A
  1. High power
190
Q
  1. What are PCr levels in resting human skeletal muscle? What is the wet muscle weight?
A
  1. ~18-20 mmol/kg, 23-26mM
191
Q
  1. Is the supply of PCr abundant or limited?
A
  1. Limited
192
Q
  1. What capacity does the phosphocreatine system have?
A
  1. Low capacity
193
Q
  1. During exercise _____ falls in proportion to the _____
A
  1. PCr, relative intensity of exercise
194
Q
  1. In all out efforts how much can PCr change by?
A
  1. Decrease by 90% or more
195
Q
  1. When does the reserve of the CK reaction dominate?
A
  1. During recovery or rest periods
196
Q
  1. Phosphate transfer to creatine from ATP produced from what regenerates what?
    1. ATP _____ process
    2. Derived from _____
A
  1. From oxidative phosphorylation regenerates PCr
    1. Consuming
    2. Aerobic metabolism

Metabolism (6 decks)

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