week 5 and week 6 ppt 1 Flashcards

1
Q

where does glycolysis take place and what is glycolysis?

A

Glycolysis takes place in the cytosol:
* Converts glucose into pyruvate
* Produces a small amount of energy* Generates no CO2

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2
Q

What is phosphorylation?

A

Phosphorylation is the addition of a phosphate group to a molecule.

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3
Q

What is substrate-level phosphorylation?

A

Phosphorylation is the addition of a phosphate group to a molecule. Substrate-level phosphorylation is an enzyme-catalyzed transfer of a phosphate group from a donor molecule to ADP, forming ATP.

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4
Q

What happens during pyruvate oxidation and where does it occur?

A

Pyruvate oxidation is the process that links glycolysis to the citric acid cycle and occurs in the mitochondrial matrix. During this process, pyruvate is oxidized to acetate, releasing CO2, and NAD+ is reduced to NADH, capturing energy. Some of the energy is stored by combining acetate with Coenzyme A (CoA) to form acetyl CoA.

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5
Q

What is the role of acetyl CoA in cellular respiration and what are the inputs and outputs of the citric acid cycle?

A

Acetyl CoA is the starting point for the eight-reaction citric acid cycle. The inputs of the cycle include acetyl CoA, water, and electron carriers NAD+, FAD, and GDP. Energy released during the cycle is captured by ADP and the electron carriers, producing the outputs CO2, reduced electron carriers (NADH and FADH2), and GTP, which can be used to convert ADP to ATP.

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6
Q

what is the equation for the metabolism of glucose?

A

C6H12O6 + 6O2 -> 6CO2 + 6H2O + free energy

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7
Q

what is he equation for the glucose metabolism pathway that traps the free energy in ATP?

A

ADP + P(i) + free energy -> ATP

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8
Q

What is oxidative phosphorylation and what are its two stages?

A

Oxidative phosphorylation is the process where ATP is synthesized by the reoxidation of electron carriers in the presence of oxygen (O2). It consists of two stages: electron transport and chemiosmosis.

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9
Q

What happens during the electron transport stage of oxidative phosphorylation?

A

During electron transport, electrons from NADH and FADH2 pass through the respiratory chain of membrane-associated carriers in the mitochondria. This flow of electrons results in a proton concentration gradient across the mitochondrial membrane, which is then used to produce ATP.

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10
Q

Why is the electron transport chain (ETC) a series of reactions rather than just one step?

A

The ETC is a series of reactions rather than just one step because a single reaction releasing the entire free energy at once would be too much for the cell to harness efficiently. By releasing energy in a series of smaller steps, each step can be coupled to an endergonic reaction, such as the synthesis of ATP, allowing the cell to capture and utilize the energy more effectively.

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11
Q

Where is the respiratory chain located and how does it contribute to ATP formation during oxidative phosphorylation?

A

The respiratory chain is located in the inner mitochondrial membrane. As electrons are passed between carriers within this chain, energy is released. This energy is used to pump protons across the membrane, creating a proton gradient. The flow of protons back into the mitochondrial matrix through ATP synthase drives the synthesis of ATP. Examples of electron carriers in the respiratory chain include protein complexes I, II, III, IV, Cytochrome c, and ubiquinone (Q).

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12
Q

What happens to protons during the electron transport phase of oxidative phosphorylation?

A

During the electron transport phase of oxidative phosphorylation, protons are actively transported across the inner mitochondrial membrane into the intermembrane space. This creates a high concentration of protons (a proton gradient) and a charge difference across the membrane, which stores potential energy known as the proton-motive force.

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13
Q

How does the proton-motive force contribute to the formation of ATP?

A

The proton-motive force, created by the proton gradient and charge difference, drives protons back across the inner mitochondrial membrane through the enzyme ATP synthase. As protons flow through ATP synthase, the potential energy is converted into mechanical energy which is then used to synthesize ATP from ADP and inorganic phosphate (Pi).

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14
Q

What is chemiosmosis and how does it facilitate ATP synthesis?

A

Chemiosmosis is the process where protons diffuse back into the mitochondrial matrix through ATP synthase, a specialized channel protein. This diffusion of protons is energetically coupled to ATP synthesis, utilizing the potential energy stored in the proton gradient to drive the production of ATP from ADP and inorganic phosphate.

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15
Q

Why is ATP synthesis favored over ATP hydrolysis within mitochondria?

A

ATP is transported out of the mitochondria once it is synthesized, which keeps its concentration within the mitochondria relatively low. This low concentration of ATP inside the mitochondria encourages the formation of more ATP.
The proton gradient necessary for ATP synthesis is continuously maintained by ongoing electron transport and active proton pumping across the inner mitochondrial membrane. This persistent proton gradient ensures a constant potential energy source for driving ATP synthesis.

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16
Q

How can ATP synthesis be uncoupled, and what role does thermogenin play?

A

ATP synthesis can be uncoupled by inserting a different H+ diffusion channel into the mitochondrial membrane, causing the energy to be lost as heat instead of being used for ATP synthesis. The uncoupling protein thermogenin, found in human infants and hibernating animals, facilitates this process. Instead of protons driving ATP synthesis via ATP synthase, thermogenin allows protons to flow back into the mitochondrial matrix without generating ATP, releasing energy as heat to maintain body temperature

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17
Q

What are the components of ATP synthase and their roles?

A

ATP synthase consists of two main components:

F0 subunit: A transmembrane channel that allows protons to flow through it.
F1 subunit: Projects into the mitochondrial matrix and houses the active sites for ATP synthesis, where ADP and inorganic phosphate are combined to form ATP

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18
Q

How is energy harvested from glucose in the absence of oxygen?

A

In the absence of oxygen, energy from glucose can still be harvested through glycolysis followed by fermentation. This process occurs in the cytosol and allows for the regeneration of NAD+ from NADH + H+, which is crucial for the continuation of glycolysis under anaerobic conditions.

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19
Q

What is lactic acid fermentation, and where does it occur?

A

Lactic acid fermentation is a process that occurs in microorganisms and some muscle cells under anaerobic conditions. Pyruvate, the end product of glycolysis, acts as the electron acceptor and is reduced by NADH + H+ to form lactate. This process regenerates NAD+, allowing glycolysis to continue. Lactate can accumulate, leading to muscle fatigue.

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20
Q

What is alcoholic fermentation, and which organisms use this process?

A

Alcoholic fermentation is a process used by yeasts and some plant cells to harvest energy from glucose in the absence of oxygen. This process requires two enzymes to convert pyruvate into ethanol. First, pyruvate is decarboxylated to acetaldehyde, which is then reduced by NADH + H+, producing ethanol, NAD+, and allowing glycolysis to continue.

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21
Q

How does the energy yield of cellular respiration compare to that of fermentation?

A

Cellular respiration yields significantly more energy per glucose molecule than fermentation. Glycolysis followed by fermentation produces a net gain of 2 ATP per glucose molecule, whereas glycolysis followed by cellular respiration can produce up to 32 ATP per glucose molecule. However, in some cells, the shuttling of NADH may use ATP, resulting in a net yield of approximately 30 ATP.

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22
Q

How are metabolic pathways interrelated and regulated?

A

Metabolic pathways are interrelated through the interchange of molecules, with many pathways sharing substances. They are regulated by enzyme activity, which can be influenced by various factors including enzyme inhibitors. This regulation ensures efficient control over the flow of substrates and the rate of product formation, maintaining metabolic balance and cellular homeostasis.

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23
Q

What are catabolic interconversions and how do they contribute to metabolic pathways?

A

Catabolic interconversions are processes where complex molecules are broken down into simpler ones, releasing energy and providing intermediates for metabolic pathways. Examples include:

Polysaccharides being hydrolyzed to glucose, which then enters glycolysis and cellular respiration.
Lipids being broken down into glycerol (which enters the pathway as dihydroxyacetone phosphate, DAP) and fatty acids (which are converted to acetyl CoA).
Proteins being hydrolyzed to amino acids, which can feed into glycolysis or the citric acid cycle.

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24
Q

What are anabolic interconversions, and how do they relate to metabolic regulation?

A

Anabolic interconversions involve the synthesis of complex molecules from simpler ones, often using energy in the process. These reactions can be the reverse of catabolic reactions, such as gluconeogenesis, where glucose is formed from citric acid cycle and glycolysis intermediates. Anabolic and catabolic pathways are integrated, allowing the cell to balance energy release with the synthesis of new molecule

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25
Q

How are catabolism and anabolism integrated and regulated within the cell?

A

Catabolism and anabolism are integrated and regulated through mechanisms like negative and positive feedback controls, which help maintain constant concentrations of biochemical molecules such as glucose in the blood. This integration ensures that energy release and the synthesis of cell components are balanced according to the cell’s needs.

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26
Q

How are key metabolic pathways like glycolysis, the citric acid cycle, and the respiratory chain regulated?

A

Key metabolic pathways such as glycolysis, the citric acid cycle, and the respiratory chain are subject to allosteric regulation of key enzymes. This means the activity of these enzymes can be modulated by the binding of molecules at sites other than the active site, which can enhance or inhibit their function. This type of regulation allows the cell to finely tune metabolic pathways in response to the cell’s energy demands and the availability of substrates.

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27
Q

What is the main control point in glycolysis and how is it regulated?

A

The main control point in glycolysis is phosphofructokinase, which is allosterically inhibited by ATP. When ATP levels are high, this inhibition slows down glycolysis, preventing the wasteful production of more ATP.

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28
Q

What regulates the citric acid cycle’s main control point.

A

The main control point in the citric acid cycle is isocitrate dehydrogenase, which is inhibited by NADH + H+ and ATP. High levels of NADH + H+ and ATP indicate abundant energy, leading to the slowing down of the cycle to prevent excessive production of energy carriers

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29
Q

How does the accumulation of citrate affect metabolic pathways when ATP levels are high?

A

When ATP levels are high, the accumulation of citrate can divert acetyl CoA away from the citric acid cycle to fatty acid synthesis for storage. Later, these fatty acids may be metabolized to produce more acetyl CoA, providing a way to store energy for future needs.

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30
Q

What are some examples of protein secretion across different organisms?

A

In microbes, an example is fungal sex pheromones.
In plants, gibberellins are secreted (though not proteins).
In mammals, an example of a secreted protein is growth hormone.

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31
Q

Why do organisms secrete proteins?

A

Organisms secrete proteins for various reasons, including:

Construction of cell walls in microbes and plants.

Extracellular degradation of nutrient sources through enzymes like lignases, cellulases, phosphatases, and lipases.

Cell communication, such as the secretion of sex pheromones in microbes and hormones in animals and plants.

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32
Q

How do hormones function in cell communication?

A

Hormones secreted by cells diffuse into the extracellular fluid and are often distributed by the circulatory system to coordinate anatomical, physiological, and behavioral changes in an animal. They play a crucial role in intercellular communication, affecting various aspects of organismal function.

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33
Q

What is the relationship between endocrine cells and endocrine glands?

A

Some endocrine cells aggregate into secretory organs known as endocrine glands. These glands are responsible for the production and release of hormones into the bloodstream, facilitating long-distance signaling and regulation within an organism.

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34
Q

What is the role of Growth Hormone (GH) and where is it synthesized?

A

Growth Hormone (GH) is synthesized and secreted by the anterior pituitary gland. It acts on many tissues to promote growth by stimulating cells to take up amino acids and stimulating the liver to produce insulin-like growth factors that promote bone and cartilage growth.

35
Q

What are the effects of GH overproduction and underproduction?

A

Overproduction of GH in children can lead to gigantism, characterized by excessive growth and height.

Underproduction of GH causes pituitary dwarfism, resulting in reduced growth and shorter stature. GH is now also produced by genetically engineered bacteria for therapeut

36
Q

What are gibberellins and their role in plant growth?

A

Gibberellins are a class of plant hormones secreted by the plant embryo. They play a crucial role in plant growth by triggering changes in the aleurone layer inside the seed coat, leading to the synthesis and secretion of enzymes that digest proteins and starch stored in the endosperm. Developing seeds produce gibberellins, which also diffuse out into the immature fruit tissue, influencing its growth and development.

37
Q

What is the function of fungal sex pheromones?

A

Fungal sex pheromones allow fungi to recognize cells of the opposite mating type, promoting mating between cells of opposite types. Examples include yeast a-factor and yeast alpha-factor, which facilitate the mating process in yeast.

38
Q

What is yeast alpha-factor?

A

Yeast alpha-factor is a short peptide processed by cleavage from a longer polypeptide.

39
Q

How is yeast alpha-factor involved in mating?

A

It is secreted from yeast alpha cells and detected by yeast a cells, promoting mating between a and alpha cells.

40
Q

What are the two main types of compartments proteins are targeted to after synthesis?

A

Intracellular compartment (nucleus, mitochondrion, lysosome, chloroplast) and extracellular compartment (periplasm, cell wall, bloodstream).

41
Q

After synthesis, where are many proteins transported?

A

From the cytoplasm to another cellular compartment such as the nucleus, mitochondrion, lysosome, chloroplast, or extracellularly to the periplasm, cell wall, or bloodstream.

42
Q

What happens during translation related to the mechanisms of secretion?

A

The newly synthesized signal sequence binds to the Signal Recognition Particle (SRP), causing translation to stall temporarily.

43
Q

What occurs after the SRP binds to the newly synthesized signal sequence?

A

The complex docks at a specific receptor on the surface of the ER, and a channel opens in the membrane.

44
Q

What indicates where in the cell a polypeptide belongs?

A

Many polypeptide sequences contain “signals” that indicate their cellular destination.

45
Q

What do secreted proteins contain that is crucial for their secretion?

A

A circa 25 amino acid, N-terminal Signal Sequence.

46
Q

What happens after the Signal Recognition Particle (SRP) disassociates from the complex in protein secretion?

A

Translation restarts, and the protein is co-translationally translocated into the lumen of the ER. The N-terminal signal sequence is then cleaved from the nascent polypeptide chain.

47
Q

How does co-translational translocation proceed after the signal sequence is cleaved?

A

Co-translational translocation continues into the ER, chaperonins refold the protein in the ER, and translation terminates with the completed polypeptide released into the lumen of the ER.

48
Q

What directs further protein sorting events after translation?

A

Other signals, such as specific retention signals for staying in the ER and sugars added in the Golgi apparatus to form glycoproteins for lysosomes or the plasma membrane.

49
Q

What happens to proteins with no further signals after post-translational modification?

A

They go through the Golgi apparatus and are secreted from the cell.

50
Q

How are glycoproteins formed and what is their destiny?

A

Sugars are added in the Golgi apparatus to form glycoproteins, which then go to lysosomes or the plasma membrane.

51
Q

What role do specific retention signals play in protein sorting?

A

They allow the protein to stay in the ER.

52
Q

Are most proteins modified before or after translation?

A

Most proteins are modified after translation.

53
Q

Why are post-translational modifications important for proteins?

A

These modifications are often essential to the functioning of the protein.

54
Q

What are the three types of post-translational modifications?

A

Proteolysis (cleaving), Glycosylation (adding sugars), and Phosphorylation (adding phosphate groups).

55
Q

What does proteolysis involve in the context of post-translational modifications?

A

Proteolysis involves the cleaving of proteins.

56
Q

What is the role of glycosylation in post-translational modifications?

A

Glycosylation involves adding sugars to proteins, which can affect their folding, stability, and activity.

57
Q

How does phosphorylation modify proteins and why is it significant?

A

Phosphorylation adds phosphate groups to proteins, playing a critical role in regulating protein function and signaling pathways.

58
Q

Why do microbial cells, animals, and plants need to sense and react?

A

To survive by responding and adapting to environmental changes, responding to external stimuli, and maintaining homeostasis through hormonal and other signals.

59
Q

How do cells receive signals?

A

Signals secreted by one cell are detected by other cells that express the corresponding receptor. Cells that do not express the receptor do not receive the signal.

60
Q

Where can receptors be located in a cell?

A

Receptors can be located at the cell surface or inside the cell.

61
Q

What are the three well-studied types of transmembrane receptors in complex eukaryotes?

A

Protein kinases, ion channel receptors, and G protein-linked receptors.

62
Q

What is the function of protein kinase receptors?

A

Some receptors become protein kinases—they catalyze the phosphorylation of themselves and/or other proteins.

63
Q

How does the insulin receptor function as a protein kinase receptor?

A

The insulin receptor phosphorylates itself and other insulin response substrates, which initiates the insertion of glucose transporters into the plasma membrane.

64
Q

What are ion channel receptors?

A

Channel proteins that allow ions to enter or leave a cell, activated by signals such as chemical ligands (hormones), sensory stimuli (light), or electric charge differences.

65
Q

Can you give an example of an ion channel receptor on muscle cells?

A

The acetylcholine receptor on muscle cells is a gated ion channel.

66
Q

How do G protein-linked receptors function?

A

Ligand binding changes the shape of the cytoplasmic region, which then binds to a G protein, a mobile membrane protein with three subunits that binds GDP and GTP.

67
Q

What happens after the GTP-subunit separates from the G protein?

A

It moves through the plasma membrane until it encounters an effector protein, activates the effector, causing a change in cell function, and GTP is hydrolysed to GDP.

68
Q

How can G proteins influence effector proteins?

A

G proteins can either activate or inhibit an effector. For example, epinephrine binds to a G protein-linked receptor in heart muscle to activate an enzyme producing cyclic AMP, while in smooth muscle cells, it inhibits the enzyme that produces cAMP.

69
Q

How can the same signal molecule have different effects in different cells?

A

The same signal molecule, like epinephrine, can activate or inhibit effector proteins in different cells, demonstrating how G protein-mediated actions can vary based on cell type.

70
Q

What are the three main components of a basic biological circuit in signal transduction?

A

Inputs (receiving signals), Wiring (transmitting signals), and Outputs (biological response).

71
Q

What characterizes direct signal transduction?

A

Direct transduction results from the action of the receptor itself on effector proteins, often involving a Protein Kinase Cascade, amplifying the response and communicating information from the plasma membrane to the nucleus.

72
Q

How does direct signal transduction provide specificity in cellular responses?

A

Many steps in the process allow for specificity—different target proteins provide variation in response.

73
Q

What is indirect signal transduction and how does it function?

A

Indirect transduction uses a second messenger to amplify the interaction between receptor binding and cellular reaction. Second messengers include cAMP, cGMP, lipids, calcium ions (Ca++), and nitric oxide (NO).

74
Q

Where is the enzyme that catalyzes the formation of cAMP from ATP located, and what are cAMP’s major target types?

A

The enzyme adenylyl cyclase is located on the cytoplasmic side of the plasma membrane. cAMP targets include ion channels in sensory cells to open them and protein kinases in the cytoplasm to start a protein kinase cascade.

75
Q

How are other second messengers like lipids derived, and what is an example involving PIP2?

A

Derived from phospholipids in the plasma membrane hydrolyzed by phospholipases. An example is PIP2, which splits into diacylglycerol (DAG) and inositol triphosphate (IP3).

76
Q

How do low Ca2+ concentrations in the cytoplasm get maintained, and what can cause their increase?

A

Low Ca2+ concentrations are maintained by active transport proteins at plasma and ER membranes. Increases can be caused by signals like IP3 or the entry of a sperm into an egg, rapidly increasing Ca2+ concentrations in the cytoplasm.

77
Q

How does an overactive IP3/DAG signal transduction pathway relate to bipolar disorder, and what inhibits it?

A

An overactive IP3/DAG pathway leads to excessive brain activity in bipolar disorder.

78
Q

What is an example of signal amplification in signal transduction?

A

Fertilization of an egg triggers a wave of calcium ions [Ca2+] that stimulates the initiation of development, demonstrating how a single event can lead to a significant biological response.

79
Q

How does the fertilization of an egg demonstrate signal amplification?

A

The fertilization triggers a wave of calcium ions [Ca2+], imaged at 5-second intervals, which stimulates the initiation of development.

80
Q

How does serotonin affect nerve cells?

A

Serotonin activates a response in nerve cells via a cAMP signaling pathway, leading to a rapid increase in intracellular cAMP concentration within 20 seconds of exposure. Serotonin is involved in pain control, sleep/wake control, and mood regulation.

81
Q

How is our sense of smell related to signal transduction?

A

Our sense of smell depends on G-protein-coupled receptors and cAMP-gated ion channels. The influx of Na+ and Ca2+ stimulates nerves to send signals to the brain, illustrating the role of G-protein-linked receptors in sensory perception.

82
Q

what are the products of glycolysis?

A

– 2 molecules of pyruvate
– 2 molecules of ATP
– 2 molecules of NADH

83
Q

how many reactions are involved in gycolysis?

A
  • Glycolysis involves ten enzyme-catalyzed reactions.
  • Energy-investing reactions one–five require ATP.
  • Energy-harvesting reactions six–ten yield NADH and ATP.
84
Q
A