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Bioenergetics > Bioenergetics > Flashcards

Bioenergetics Flashcards

1
Q

Bioenergetics

A

Study of the transformation of energy in living organisms

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2
Q

Metabolism

A

Sum of all chemical reactions in the body

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3
Q

Catabolic

A

Breakdown/ degradation of molecules

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4
Q

Examples catabolic

A

Proteolysis, lipolysis, glycolysis, glycogenolysis

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5
Q

Anabolic

A

synthesis of new molecule

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6
Q

Examples of anabolic

A

protein synthesis, lipogenesis, gluconeogenesis, glycogenesis

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7
Q

How are enzymes pathways regulated?

A

• substrate supply - food & other compounds
• hormonal control - with on/off pathways & alter enzyme activity
• allosteric control - speed or slow enzyme activity

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8
Q

ATP

A
  • Fuels body
  • used metabolic reactions
  • all stores used up in 2-4 seconds
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9
Q

How do we generate ATP?

A

• metabolic reactions rely on enzymes
• enzymes speedup reactions
• enzyme lower activation energy, initial energy required for the reaction to take place LG

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10
Q

Lock & Ky

A

binding site has complementary shape to substrate(s)

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11
Q

Induced fit models

A

contact between part of the binding site and the substrate induces a change in shape of the active site to bind to the substrate

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12
Q

Enzyme activity can be affected by

A

• Substrate concentration
• pH
• Temperature
• Enzyme concentration

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13
Q

Atom

A

Building block

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14
Q

Element

A

pure substance which cannot be broken down into a simple substance by a chemical reaction

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15
Q

Proton

A

+ charge
In nucleus

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16
Q

Neutron

A

Neutral chase
in nucleus

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17
Q

Electron

A

Negative charged
Outer shell

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18
Q

Ion

A

atom becomes an ion when it is charged has been altered by losing or gaining an election

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19
Q

Anion

A

Negative charged ion

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20
Q

Cations

A

Positive charged ions

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21
Q

Molecule

A

contains two or more atoms chemically joined together

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22
Q

Compound

A

molecule composed of atoms from 2 or more different elements

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23
Q

Ionic bonds

A

Ionic bonds
• giving an electron to another atom/receiving an electron from another atom
• depends on electronegativity

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24
Q

Covalent bond

A

sharing electrons with another atom
• shared electrons between atoms fill shells

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25
Q

Order of strongest bond

A

Covalent > ionic > hydrogen

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26
Q

Redox reaction

A

If one molecule is oxidized, the other is reduced

When we generate large amounts of ATP, oxygen accepts electrons

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27
Q

Cytoplasm

A

• fluid in cell
• cytosol is fluid portion & energy generating reaction take place

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28
Q

Mitochondria

A

• organelle - site of respiration
• generates ATP
• Exercise increases the size of the mitochondria in the cell and also the number it contains

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29
Q

Cell membrane

A

The gatekeeper of the cell!
• Surrounds the whole cells
• Lipid bilayer – phospholipid, glycolipid, cholesterol

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30
Q

How does phosphocreatine system synthesise ATP?

A
  • Breakdown of ATP to ADP activates creatine kinase
  • enzyme catalyses reaction that adds pi group
  • can resynthesises PCr quickly
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31
Q

Oxygen deficit

A
  • Due to rapid need for energy
  • energy comes from non-aerobic sources
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32
Q

PCr depletion

A

Only have finite stores hence why people take creatine supplements

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33
Q

Which metabolic pathways are activated during very high intensity exercise?

A
  • Phosphocreatine
  • anaerobic glycolysis
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34
Q

What is the PREDOMINANT pathway activated for a given task; these pathways NEVER work in isolation

A

Glycolysis

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35
Q

The metabolic pathways activated during intermittent exercise such as team sports

A
  • Glycolysis
  • krebs
  • ETC
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36
Q

possible causes of fatigue during high-intensity during high intensity and intermittent exercise

A

stores of PCr limited
Increase in ADP inhibits

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37
Q

glycolysis

A

breakdown of glucose to produce energy

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38
Q

what hormones regulate glycolysis

A

insulin(activator) and glucagon(inhibitor)

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39
Q

What happens in anaerobic conditions

A

Build up in pyruvate increases lactic acid production

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40
Q

How much ATP does glycolysis produce

A

2 ATP (net)

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41
Q

How much NADH is produced in glycolysis

A

2

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42
Q

glycogenesis

A

formation of new glycogen
addition of glucose molecules together to form branches

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43
Q

glycogenolysis

A

breakdown of glycogen
break of glucose molecule

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44
Q

muscle stores of glycogen

A

2% by weight is glycogen
largest store in body
released as glucose-6-phosphate

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45
Q

liver stores of glycogen

A

10% by weight is glycogen
controls blood glucose levels

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46
Q

phosphorlysis

A

breaking up of glycogen molecule by adding phosphoric group

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47
Q

glycogen

A

can only be stored as branches of glucose polymer
having several branches means that they be broken down for glucose molecule

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48
Q

Krebs cycle

A

eight reactions in mitochondria
is an aerobic process

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49
Q

function of Krebs cycle

A
  • oxidation pathway for carbs, lipids, proteins
    -generate energy or intermediates for ETC
  • provides several precursor molecules for other metabolic pathways
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50
Q

link reaction

A

converts pyruvate to acetyl coenzyme A

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51
Q

When is the Krebs cycle activated?

A

when oxygen is present
PDH activates it

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52
Q

what enzyme regulates links reaction

A

PDH

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53
Q

When is PDH activated

A

exercise
PDH phosphatase

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54
Q

when is PDH inhibited

A

PDH kinase
exercise

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55
Q

What is the starting molecule I Krebs cycle and what do you end up with

A

Starts- acetyl coenzyme A
Ends- Oxaloacetate

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56
Q

How much ATP produced in one cycle

A

1

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57
Q

NADH and FADH2 production in Krebs cycles

A

NADH-3
FADH2- 1
used in ETC

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58
Q

ETC

A

redox reaction

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59
Q

substrate level phosphorylation

A

generate ATP from both glycolysis and Krebs

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60
Q

oxidative phosphorylation

A

process of using high energy electron carries to generate ATP

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61
Q

how is ETC regulated

A

Hormonal or allosteric regulation absent
increase in NADH, ADP, Pi

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62
Q

How much ATP is produced in ETC

A

38

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63
Q

Where does ETC happen?

A

mitochondria

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64
Q

What are the roles of NADH and FADH2 in ETC?

A

electrons from coenzyme used for redox reaction

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65
Q

How does the protein complex on ETC function- where is the electron affinity greatest?

A

electrochemical gradient that leads to the creation of ATP
final electron acceptor

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66
Q

how is ETC regulated?

A

by the proton gradient between the inner membrane and the mitochondrial matrix

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67
Q

What types of exercise utilise the ETC?

A

low-intensity long endurance

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68
Q

characteristics of protein showing sigmoidal kinetics

A
  • composed of 2 or more sub units
  • subunits can exist in 2 different shapes
    -first substate binds to site and increases affinity for 2nd substrate
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69
Q

Allosteric protein

A

binding of the negative effector to its ligand binding site prevents the enzyme’s active site from becoming accessible to the substrate

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70
Q

Positive modulator

A

binding of the positive effector to its ligand binding site makes the enzyme’s active site more accessible to the substrate

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71
Q

Gluconeogenesis

A

takes place in the liver
several substrate covered to glucose

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72
Q

When is Gluconeogenesis activated?

A

After 30-40 minutes of exercise when energy in the body is low because glucose hasn’t been consumed

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73
Q

What tissue does Gluconeogenesis occur in?

A

Liver

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74
Q

How many irreversible reactions in glycolysis does gluconeogenesis have to overcome?

A

3 reaction

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75
Q

What substrates can be used in Gluconeogenesis?

A

Lactate, amino acid( glutamine & alanine) glycerol

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76
Q

pentose phosphate pathway

A

can be used to oxidase glucose
no ATP required
NADPH formed

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77
Q

What are the end products of pentose phosphate pathway?

A

phosphate and pentose

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78
Q

how is pentose phosphate pathway regulated?

A

redox state of the NADP couple

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79
Q

what is the free amino acid pool and what feeds into it?

A
  • substrates of protein synthesis and the products of protein breakdown
  • food and protein degradation
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80
Q

What is transamination?

A

enables all AA to be formed
transferring amine group to a keto acid to for AA

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81
Q

What is oxidative deamination

A

removing the amine group from a newly AA resulting is transamation

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82
Q

What is the urea cycle?

A

Any AA body doesn’t used are removed in liver
degrading AA convert to ammonia
ammonia converted to urea in the liver
excreted through kidney

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83
Q

protein synthesis

A

formation of new proteins

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84
Q

protein degradation

A

breakdown of proteins into AA’s

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85
Q

how much protein do we lose a day?

A

35-100g

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86
Q

Why is protein synthesis important for athletes ?

A

Muscle hypertrophy
help with resistance training

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87
Q

transcription

A

copy information encoded in a gene and duplicate it

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88
Q

translation

A

form the amino acids chain, rely on genetic code

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89
Q

codons
anti codons
tRNA

A

codons- RNA triplet codes
anti codons - complementary codon on tRNA
tRNA- carry amino acid

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90
Q

What are the 2 pathway for protein degradation?

A

lysosomal pathway and ubiquitin pathway

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91
Q

Saturated fatty acids

A

no carbon double bonds
straight, tightly packed
solid at room temp

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92
Q

unsaturated fatty acids

A

at least 1 carbon double bond
less tightly packed
liquid at room temp

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93
Q

mono and poly unsaturated

A

mono- one double bond
poly- more than one

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94
Q

lipoproteins

A

lipids surrounded by protein
after digestion used to transport lipids around the body to different tissues

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95
Q

lipolysis

A

breakdown of TAG into 3 fatty acids and 1 glycerol
each fatty acid broken down by different hormone
regulated by enzymes

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96
Q

What activates lipolysis during exercise?

A

adrenaline

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97
Q

What are the different hormones that break down fatty acids?

A

ATGL
HSL
MGL

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98
Q

When is ATP generation with lipids more than carbs?

A

all the time but takes longer

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99
Q

Beta-oxidation

A

carbon chains of fatty acid removed
obtain acetyl coenzyme A
occurs in mitochondria matrix
requires oxygen

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100
Q

What does malonyl CoA do and why is it revenant?

A

Is an enzyme that joins acyl and carnitine together
important regulator of CAT1 activity

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101
Q

Fatty acid synthesis

A

Acetyl CoA synthesised to form malonyl CoA
by Acetyl CoA breaks into OAA and citrates
citrate then breaks into OAA and CoA
CoA converted to maloynl CoA

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102
Q

What molecule is an important regulator of FA synthesis and FA degradation

A

ACC (Acetyl-CoA carboxylase

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103
Q

Under what circumstances would FA be promoted?

A

After eating due to an increase in fatty acids and increase in insulin released

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104
Q

how are triglycerides formed?

A

insulin promotes the uptake of fatty acids and glucose into adipose tissue
in adipose tissue glucose covered with glycerol and 3 fatty acids form ester bonds with glycerol

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105
Q

What are ketone bodies?

A

the fuel source for the brain when glucose low
used when high fatty acids are in use
e.g acetoacetic acid, 3-hydroxybutyric, acetone

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106
Q

When are ketone bodies increased in the body?

A

during hunger
reduced carb availability
starvation
prolonged exercise

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107
Q

hormones

A

the chemical messenger that regulates and coordinate activity within the body

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108
Q

Endocrine hormones

A

produced in one tissue
travel through circulation to reach the target cell

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109
Q

Paracrine hormones

A

produced in one cell
travels short distance to neighbouring target cells

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110
Q

Autocrine hormones

A

produced in cell which is also target cell

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111
Q

kinase

A

adds phosphate group to substrate

112
Q

phosphatase

A

removes phosphate group from substrate

113
Q

phosphorylase

A

transfer inorganic phosphate to substrate

114
Q

hormonal cascade

A

stimulus- CNS- hypothamlus- anterior pituitary-specific target endocrine gland- metabolic effects

115
Q

endocrine hormones differ in…

A
  • solubility
  • mechanism in action
  • speed of action
116
Q

steroid hormones

A
  • transport in the blood bound to specific transport proteins
  • binds to a receptor on the cell surface
  • hormone enters the target cell
  • binds to specific receptors within cell
  • hormones receptor complex binds to specific regions of DNA
  • influence transcription
117
Q

Peptide and catecholamine hormones

A
  • transport in free form in blood
  • bind to specific cell surface receptors
  • hormones doest enter cell
  • second messenger model
118
Q

glucagon

A
  • released from alpha cells in pancreases
  • signals lack of glucose
  • main target is liver and adipose tissue
119
Q

adrenaline

A
  • synthesis in adrenal gland
  • released in fight or flight response
    provides source of energy to tissues in times of stress
120
Q

G protein activation of adenylate cyclase

A
121
Q

insulin

A

released from B cells of pancreas
signals high plasma glucose
main target in liver and skeletal muscles

122
Q

tyrosine specific kinases

A

transmembrane receptor proteins
when ligand binds there is change in shape
initiates cascades

123
Q

PIP3-PKB casade

A
124
Q

What does the binding of glucagon cause?

A

induces a conformational change in the intracellular part of the receptor which results in interaction with other proteins in the membrane to effect enzyme activity

125
Q

What is glucagon receptor

A

Gsa

126
Q

What is adrenaline receptors and what do they imitate?

A

beta adrenergic - cAMP-PKA pathway
alpha adrenergic - phospholipase C-PKC pathway

127
Q

what does adrenaline cause?

A

decrease blood flow to skin
contracts smooth muscle in skin
cause smooth muscle in lungs to relax
causes increase in heart rate

128
Q

what is insulin receptor ?

A

tyrosine receptor kinase

129
Q

what does insulin stimulate?

A

glycogenesis and lipogenesis

130
Q

Adipose- carb metabolism

A

Energy production
Nadph production
Glycerol phosphate production

131
Q

Adipose - lipid metabolism

A

Fatty acid synthesis
Acylylycerol synthesis
Lipolysis
Energy production

132
Q

Muscle-carb metabolism

A

Glycogen synthesis/ degradation
Energy production

133
Q

Muscle-lipid metabolism

A

Energy production

134
Q

Muscle -protein metabolism

A

Protein synthesis/ degradation
Alanine production

135
Q

Liver-carb metabolism

A

interconversion of monosaccharides
glycogen synthesis/degradtion
energy production
gluconeogenesis
pentose metabolsim

136
Q

Liver- lipid metabolisim

A

fatty acid synthesis
energy production
ketone body formation

137
Q

Liver- protein metabolism

A

transamination/ deamination
protein synthesis
urea cycle

138
Q

what is the responsibility of insulin?

A

uptake and utilisation and storage of nutrients when concs of blood rise
e.g blood conc are not too high

139
Q

What s the responsibility of glucagon?

A

raising blood glucose concentrations if they fall too low
cause other nutrietns to be used as a source of energy
main target is liver and adipose tissue

140
Q

Insulin effect on the liver

A

stimulates glycogenesis
inhibits glycogenolysis

141
Q

insulin effect on muscle

A

stimulate glucose uptake
stimulates glycogenesis
inhibits glycogenolysis

142
Q

insulin effect on adipose

A

stimulates glucose uptake
stimulate lipogenesis
inhibits lipolysis

143
Q

Glucagon &adrenaline effect onliver

A

stimulate glycogen degradation
inhibit glycogen synthesis
increase blood glucose

144
Q

Glucagon &adrenaline effect on muscle

A

no glucagon receptor
stimulate glycgoen degradtion
inhibit glycogen synthesis
increase energy from glucose

145
Q

Effect of insulin, glucagon, adrenaline on lipolysis in adipose

A

degradation of TAG each stage releases a fatty acid
glucagon and adrenaline activate ATGL and HSL
insulin inhibits ATGL and HSL

146
Q

what does the iron in haem do?

A

cause the binding of oxygen

147
Q

Myoglobin

A

single molecule
found in muscle
high affinity of oxygen

148
Q

Haemoglobin

A

4 sub units- alpha and beta
can bind to 4 o2
binding curve is sigmoidal

149
Q

What kinetics does myoglobin follow

A

Michaelis-Menton Kinetics of oxygen binding

150
Q

Michaelis-Menton Kinetics of oxygen binding

A

high saturation with oxygen at high ppo2
relsease o2 as ppo2 falls

151
Q

Haemoglobin affintity

A

High saturation of Hb with o2 at po2 of lung
low saturation of Hb at po2 of tissues so o2 is released at tissues

152
Q

Allosteric effector for haemoglobin

A

BPG acts as a negative effector
so more oxygen is delivered to tissues
BPG conc increases when insufficient oxygen is getting to tissues

153
Q

foetal haemoglobin

A

made of 4 units- alpha and gamma
binds to oxygen more strongly because of low affinity to BPG
as oxygen has to travel from maternal blood to foetal blood

154
Q

Sarcomere

A

made up of thick and thin myofilaments
stretches between 2 Z discs
leads to different density under microscope

155
Q

thin filaments

A

protein actin
polymerises to form long strands which then form a 2-standed helical filement
F actins capped to prevent elongation
troponin and tropomyosin- both attached

156
Q

thick filemants

A

protein myosin
2 identical heavy and 4 light chains
head domains specialised to ATPases

157
Q

muscle contraction initated by?

A

calcium

158
Q

Stage 1 muscle contraction

A

ATP binds to myosin head causing myosin to lose affintiy for actiin

159
Q

Stage 2 muscle contraction

A

myosin head folds around th ATP causong flexion on myosin molecule neck
ATP is hydrolyed to ADP & Pi
Head binds to new actin sub-unit

160
Q

Stage 3 muscle contraction

A

Pi released from myosin caused conformational change
power stroke- allows myosin to return to original conformation

161
Q

Stage 4 muscle contraction

A

ADP released to complete cycle

162
Q

What transmitter is used to send signal from nerve to muscle?

A

acetylcholine

163
Q

Where is calcium released from?

A

In response to nerve stimulus it is released from sarcoplasmic reticulum

164
Q

How is calcium returned to sarcoplasmic reticulum?

A

Ca/ATPase

165
Q

When do the Na+ released in muscle contraction?

A

when impulse flows down nerve

166
Q

What happens once Na+enters axon?

A

depolarisation due to voltage-gated Ca2+ channels
Ca2+ flows into axon terminal releases acetylcholine
acetylcholine passes over synatpic cleft binds to receptors on muscle cells

167
Q

What does acetylcholine bind to?

A

Nicotinic acetylcholine receptors

168
Q

What happens once acetylcholine reaches muscle cell receptors?

A

Na+ and K+ enter depolarising the membrane
voltage gated Na+ channels all throughout till linked T-tubules
activates protein in t-tubule

169
Q

What happens once Ca2+ is released from channels into sarcoplasm?

A

binds to TN-C
which initates muscle contraction

170
Q

How many carbon atoms does a molecule of fructose contain?

A

6

171
Q

Which transporter sits at the contraluminal side of the epithelial cells in the small intestines to assist in the absorption of carbohydrates?

A

Glut 4

172
Q

Where does the digestion of lipids/fat start and what is the name of the enzyme?

A

Mouth; lipase

173
Q

Without the presence of co-morbities, what does the body mass index (BMI) of a person need to be in order to qualify for bariatric surgery?

A

> 35

174
Q

Is gastric band procedure a reversible procedure

A

Yes

175
Q

In what bariatric surgery, what is the name of the surgery called where a large part of the stomach is bypassed by attaching the top of the stomach is attached to the small intestine?

A

Roux - en Y

176
Q

Bypass surgery can increase the risk of malnutrition due to incomplete digestion and absorption. Malnutrition of which of the following nutrient is least likely to occur following bypass surgery?

A

Carbs

177
Q

Insulin is secreted in which specific cells?

A

Beta-cells in pancreas

178
Q

Insulin stimulates the activity of what enzyme at the site of adipose tissue to 1. take up triglycerides derived from food into the tissue and 2. inhibit the release of free fatty acids into the blood.

A
  1. lipoprotein lipase 2. Hormone-sensitive lipase
179
Q

How much is the energy potential that is stored in liver glycogen?

A

400 kcal

180
Q

A patient has a blood glucose concetration at the end of the 2h OGTT of 10.9 mmol/L. In what category does this patient fall in terms of blood glucose homeostasis?

A

Impaired glucose tolerance

181
Q

Glucagon triggers a(n) [1] in blood glucose concentrations. The [2] is the responsible organ for this effect. The condition in which this metabolic response occurs is in the [3]

A
  1. Increase 2. Liver 3. Postabsorptive state
182
Q

What is the main energy source that a 100-m sprint athlete uses during their sport?

A

ATP-PCr

183
Q

Which of these best illustrates the definition of metabolism?

A

The sum of all reactions in the body

184
Q

Your friend is deficient in iron, what micronutrient would you recommend they start to consume alongside iron-rich foods?

A

Vitamin C

185
Q

What are the 4 most common elements in living things?

A

Carbon, oxygen, nitrogen, hydrogen

186
Q

Which of these is an anabolic reaction?

A

Gluconeogenesis

187
Q

How do enzymes speed up metabolic reactions?

A

Lower the activation energy

188
Q

Positively charged ions are known as

A

Cations

189
Q

The chemical formula of glucose is C6H12O6. How many molecules, elements and atoms does glucose have?

A

1 Molecule, 3 elements and 24 atoms

190
Q

What are the 3 main ways that metabolism is regulated?

A

Substrate control
Hormonal control
Allosteric control

191
Q

How much ATP do we have stored in the muscle in grams?

A

40-50

192
Q

Name 3 mechanisms of fatigue during high intensity exercise

A

PCr depletion
Reactive oxygen species
Sodium-potassium dysfunction

193
Q

When performing exercise involving, several, maximal, repeated sprints (e.g., hockey or basketball), lipids are the predominant compounds oxidized to provide energy? TRUE OR FALSE

A

False

194
Q

What are the two main hormones that regulate glycolysis?

A

Insulin & glucagon

195
Q

Which is the activator and which is the inhibitor out of insulin and glucagon?

A

activator- insulin
inhibitor- glucagon

196
Q

Conversion of pyruvate to acetyl CoA:

A

is irreversible

197
Q

What is glycogenolysis?

A

breakdown of glycogen

198
Q

Complete the following: In glycolysis….

A

There are three irreversible reactions

199
Q

Fill in: Pyruvate phosphatase [1] pyruvate dehydrogenase (PDH)

A

Activates

200
Q

In the TCA cycle, 3 NADH molecules are produced: TRUE & FALSE

A

True

201
Q

Where in the cell is the electron transport chain located?

A

Inner membrane of the mitochondria

202
Q

Do we generate more energy from oxidative or substrate level phosphorylation?

A

oxidative

203
Q

Does throwing a shot put derive energy from substrate level phosphorylation or oxidative phosphorylation?

A

Substrate

204
Q

Which of the following is a catabolic reaction involving carbohydrate?

A

Glycogenolysis

205
Q

In which part of the cell does the TCA cycle take place?

A

mitochondria

206
Q

Which of these best describes covalent bond formation:

A

Electrons are shared between the atoms

207
Q

Full PCr resynthesis occurs within 1-3 minutes. Is this statement true or false?

A

False

208
Q

One full cycle of the TCA cycle generates:

A

1 ATP, 3 NADH, 1 FADH2

209
Q

Which of these statements about the electron transport chain is NOT true:

A

A cellular increase in NAD+ and ATP encourages the electron flow through the chain

210
Q

Gluconeogenesis refers to:

A

The formation of glucose from non-carbohydrate

211
Q

During prolonged aerobic exercise, such as a marathon race what is malonyl CoA

A

Malonyl CoA will be inhibited

212
Q

Describe the difference between transcription and translation and identify in which cell organelle the latter process takes place

A

Transcription is when information is copied from a gene to form mRNA. This mRNA is taken to the ribosomes, where translation takes places. Translation is the formation of new proteins

213
Q

Name 3 biological functions of proteins:

A

Enzymes, hormones, structural

214
Q

What do we call a chain of amino acids linked together?

A

protein

215
Q

Transamination involves transferring an ……. to a ….. to form a new amino acid

A

a-amino group
keto acid

216
Q

Aminotransferases are enzymes that:

A

Catalyse the reaction that produces new amino acids in transamination

217
Q

Building bigger muscles (Hypertrophy) is dependent on the balance between protein ….. and protein
……

A

synthesis
breakdown

218
Q

Protein translation takes place in which organelle of the cell?

A

ribosome

219
Q

After a resistance exercise session, messenger-RNA is increased true or false?

A

true

220
Q

What are the two main pathways for muscle protein degradation in the body?

A

Ubiquitin pathway
Correct answer
Lysomal pathway

221
Q

Which one of the below codons is the most common ‘start codon’ for protein translation?

A

AUG

222
Q

The rate of carbohydrate oxidation is highest at which of the following exercise intensities?

A

85% of VO2max

223
Q

Name a sporting event in which ATP is derived mostly derived from the ATP-phosphocreatine (PCr) pathway?

A

100m sprint or shot putt

224
Q

Ketone bodies can be used as an alternative fuel source when glucose levels are low. Which two of these molecules are ketone bodies?

A

3-hydroxybutyrate
Acetoacetate

225
Q

Why is the ATP yield from a lipid molecule much greater than from a carbohydrate molecule?

A

contains more carbons

226
Q

Identify 3 metabolic pathways associated with carbohydrate metabolism.

A

Glycolysis

Glycogenolysis

Glycogenesis

Gluconeogenesis

227
Q

Name at least 3 functions of proteins in the body.

A

Form new muscle cells

Form synthetic pathways

Form plasma proteins, immune cells and haemoglobin

Form new enzymes

Form DNA

228
Q

Identify 3 non-carbohydrate substrates that can be converted to glucose to produce ATP.

A

Alanine

Lactate

Glutamine

Glycerol

229
Q

What are the two major pathways for protein degradation in the body and after what types of exercise are they likely to be highly active?

A

Lysomal pathway

Ubiquitin pathway

Exercise that causes muscle damage

230
Q

If glucose is not provided from food or fluids, name 3 metabolic pathways that will become more activate to supply ATP?

A

Lipolysis

Gluconeogenesis

Pentose phosphate pathway

Glycogenolysis

231
Q

What is the major metabolic pathway responsible for producing ATP during 1) a vertical jump, 2) a 400 m running race, and 3) a stage race in the Tour de France?

A

Vertical jump – ATP-PCR

400 race – anaerobic glycolysis (glycolysis will do)

Tour de France race – aerobic metabolism/oxidation/electron transport chain/oxidative phosphorylation/beta-oxidation.

232
Q

Place the following metabolic pathways in order of which produces the most to least ATP molecules

A

Most - Electron transport chain

TCA cycle

Least - Pentose phosphate pathway

233
Q

Does lipolysis increase or decrease during high intensity exercise? and what are the main causes of this change?

A

Lipolysis decreases as exercise intensity increases

In part due to redistribution of blood flow to the exercising muscles as opposed to adipose tissue

Transport of fatty acids into the mitochondria for oxidation is inhibited

Reduction in carnitine available to react with acyl CoA to be transported into the mitochondrial matrix

234
Q

Name at least 3 ways in which metabolic pathways are controlled (upregulated/inhibited) in the body?

A

By hormones

By the supply of substrates

By allosteric activation

By the nervous system

235
Q

What is the difference between an endocrine, paracrine and autocrine hormone?

A

Endocrine - produced in one tissue (gland) and travel through circulation to reach a target cell which has a receptor for that hormone

Paracrine hormones – produced in one cell and travel only a short distance to reach a neighbouring target cell which has a receptor for that hormone

Autocrine hormones – produced in a cell which is also the target cell for that hormone

236
Q

Identify 2 oxygen carrying proteins and describe the main function in the body of at least one of these proteins

A

Myoglobin and haemoglobin

Myoglobin stores oxygen in the muscle

Haemoglobin transports oxygen from the lungs to the tissue

237
Q

Describe the physiological explanation why an individual is not able to sprint a marathon.

A

Energy demand (rate of energy generated per time unit) is very high during sprinting

Rate of energy supply to meet demand has to come from PCr, which has limited storage, and glycolysis, which in absence of oxygen is converted to lactate and produces H+ in the reaction. A drop in pH is a cause of fatigue.

So, reaching task failure quickly. To prevent task failure, body has to use other (aerobic) systems but the rate of energy supply is much lower, meaning that running speed has to be lowered.

238
Q

Which of the following metabolic processes is a catabolic reaction?Proteolysis
Glycogenesis
Lipogenesis
Protein synthesis

A

Proteolysis

239
Q

Organic compounds contain carbon. Is this statement true or false?

A

true

240
Q

Atoms are made up of neutrons, protons and which other component?

A

electrons

241
Q

Adaptations to aerobic exercise incluldes:

A

An Increase in the number and size of mitochondria in the cell

242
Q

Approximately how many grams of ATP do we have stored in the muscles?

A

40 – 50 grams

243
Q

Which of the following sporting events require higher amounts of free fatty acids be metabolized for energy, also known as lipolysis?

A

An ultra-marathon running race

244
Q

At which of the following exercise intensities do the highest absolute rates of fat oxidation occur?

A

60 – 70 % of VO2max

245
Q

Which molecule acts as a shuttle by transporting free fatty acids into the mitochondrial matrix for fat oxidation?

A

Carnitine

246
Q

Select the correct statement. Fatigue during prolonged duration, aerobic exercise, such as a marathon race, occurs because:

A

Depletion of glycogen stores

247
Q

Which of the following statements regarding glycolysis is true?

A

It is the predominate energy pathway activated during a 400 m running race

248
Q

Which of the following metabolic pathways generates the least number of net ATP molecules?

A

Gluconeogenesis

249
Q

While running the London marathon running race, most of the ATP would be derived from which of the following energy pathways?

A

Oxidative phosphorylation

250
Q

Which of these hormones INCREASES if you drink a carbohydrate sports drink during exercise? (1 Mark)

A

Insulin

251
Q

Which of these metabolic pathways is activated during aerobic exercise?

A

Lipolysis

252
Q

The intermediate, NADH, is converted to NAD+ in which type of chemical reaction?

A

Oxidation reaction

253
Q

Which of the below is a key enzyme for glycolysis activation during high intensity exercise?

A

Phosphofructokinase

254
Q

Select the correct answer from the options below: Glycolysis….

A

Has 10 stepwise reactions

255
Q

The ‘link’ reaction in the tricarboxylic (TCA) cycle involves which two molecules? Select two.

A

Pyruvate
Acetyl CoA

256
Q

Creatine kinase is an enzyme that catalyzes the reaction for which metabolic energy pathway?

A

PCr system

257
Q

Lipolysis is:

A

The breakdown of triglycerides

258
Q

What is the name of the enzyme that breaks down glycogen for oxidation during glycogenolysis?

A

Glycogen phosphorylase

259
Q

What is the name of the enzyme that sits at the end of the electron transport chain and transports hydrogen ions into the mitochondria for oxidation?

A

ATP synthase

260
Q

Which of the following statements about energy generation through the electron transport chain is correct?

A

At complex I, NADH is oxidized to NAD+

261
Q

Transcription is the process by which mRNA is taken from the nucleus to form a new protein true or false

A

false

262
Q

If a cell has a low energy status, such as when fasting, which of the following molecules will be accumulating?

A

ADP

263
Q

Select the correct statement from the options below: Glycogenesis is….

A

The formation of glycogen for storage

264
Q

The ‘link reaction’ is catalyzed by which enzyme?

A

Pyruvate dehydrogenase

265
Q

The molecule malonyl CoA inhibits beta-oxidation. Is this statement true or false?

A

true

266
Q

Select the correct answer from the options below: Transamination is …

A

Is the process by which other amino acids are formed

267
Q

Which of these best describes how paracrine hormones function?

A

They are produced in one cell and travel only a short distance to reach a neighboring target cell

268
Q

Steroid proteins are transported in blood bound to specific transport proteins. Is this statement true or false?

A

true

269
Q

In response to the nerve stimulus Ca2+ is released from which part of the cell to initiate muscle contraction?

A

Sarcoplasmic reticulum

270
Q

Which of the following best describes the role of myoglobin?

A

Stores oxygen in the muscle

271
Q

In muscle contraction, when Na+ enters the muscle through the acetylcholine receptor it [Blank] the membrane? Select the missing word from the options below.

A

Depolarises

272
Q

Describe 3 steps that are part of the process of lipolysis

A
  1. Triglycerides breaks down to diacylglycerol (catalysed by Adipose triglyceride lipase)
  2. diacylglycerol breaks down to monoacylglycerol (catalysed by hormone sensitive lipase)
  3. Monoacylglycerol breaks down to glycerol and fatty acid (catalysed by Monoacylglycerol lipase)
273
Q

What is the net energy yield in gluconeogenesis, glycolysis and the TCA cycle

A

Gluconeogenesis = -6 ATP

TCA cycle = 1 ATP

Glycolysis = 2 ATP

274
Q

When is gluconeogenesis activated, what are the substrates involved, and where does this process take place?

A

Activates after 30-45 mins of steady state exercise or when fasting/hungry/haven’t eaten for a while/glucose availability in the cell is low

Lactate, amino acids and glycerol can be used to generate glucose in gluconeogenesis

This process takes place in the liver

275
Q

Describe the basic structure of skeletal muscle.

A

Made up of bundles of long, thin, multinucleated cells called muscle fibres (myofibres)

These are filled with cell cytoplasm called sarcoplasm

Sarcoplasm filled with tightly packed structures called myofibrils

Myofibrils consist of a large number of contractile units called sarcomeres

A sarcomere is composed of a number myofilaments of two types – light or thin (actin) and heavy or thick (myosin)

276
Q

What are allosteric enzymes and how do they function in metabolism.

A

Allosteric enzymes bind to ligand binding sites other than the active site and in doing so alter the activity of the other ligand binding sites on the molecule, either deactivating or activating them, therefore altering their function and affinity.

Binding of effector influences affinity of the protein sub-units for the ligand

Positive effectors increase affinity

Negative effectors decrease affinity

Allosteric enzymes show cooperativity and sigmoidal kinetics

Bioenergetics (1 decks)

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