sammanfattning på allt viktigt Flashcards

1
Q

enzymes

A

large biomolecuels that acts as a catalyst to catalyze reactions, they increase reaction rates without being used up. all enzymes are proteins but not all proteins are enzymes.

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2
Q

simple enzymes

A

do not need help by non-protein components to fulfill its job

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3
Q

complex enzymes

A

need non-protein components like cofactors (inorganic compound) or coenzymes (organic compound)

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4
Q

is cofactor an organic or inorganic compound?

A

inorganic compound

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5
Q

is coenzyme an organic or inorganic compound?

A

organic compound

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6
Q

is it true that enzyme that needs cofactor is not functional without it?

A

yes

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7
Q

apoenzyme

A

enzyme without cofactor or prosthetic group but has a coenzyme. when it binds to an coenzyme it becomes active apoenzyme

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8
Q

holoenzyme

A

enzyme with cofactor and/or prosthetic group

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9
Q

carboxylation

A

adding a carboxyl group to a molecule. this process is important in many biochemical reactions, including photosynthesis and the production of certain amino acids.

carboxyl group = COOH

it is a process where carbon dioxide (CO2) is used to turn a molecule into a carboxylic acid. this means that a substance is treated with carbon dioxide in order to produce a type of acid called a carboxylic acid.

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10
Q

enzyme acitivty

A

refers to how well enzyme can do its job which is to speed up chemical reactions in the body

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11
Q

name the specific enzyme activations:

A
  • allosteric regulation
  • proteolytic cleavage
  • covalent modification
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12
Q

What is reversible competitive inhibition and how does it affect the efficiency of an enzyme?

A

Reversible competitive inhibition is a type of inhibition where an inhibitor molecule competes with the substrate for the same binding site on the enzyme.

This competition means that the enzyme can still work, but requires more substrate to do so, which can make the enzyme less efficient.

Essentially, the inhibitor is preventing the substrate from binding to the enzyme as effectively, reducing the rate of the reaction.

However, because the inhibition is reversible, if the concentration of substrate is increased, the inhibition can be overcome and the enzyme can return to its normal level of activity.

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13
Q

covalent modification

A

is used to change the structure of the enzyme. this is done by adding additional structures with a covalent bond. one example of this is phosphorylation where a phosphate molecule is added to activate the enzyme.

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14
Q

zymogen

A

is an inactive form of an enzyme that requires a biochemical change to become active.

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15
Q

proteolytic cleavage

A

is a process where a protein is cut into smaller pieces by an enzyme called protease. this process is important because it can activate or deactivate certain enzymes. when the enzyme is cut, it exposes the active site, which is the part of the protein where other molecules can bind and interact with it. the protease cuts the protein at specific points called cleavage sites to produce smaller peptides or proteins.

some enzymes are intially produced in an inactive form and require proteolytic cleavage to become active.

one example is the enzyme pepsin that begins as an zymogen and needs to be cleaved into smaller pieces before it can function.

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16
Q

name all the different specific enzyme inhibtions

A

reversible competitive inhibition
allosteric inhibition
uncompetitive inhibition
mixed inhibition
irreversible competitive inhibtion
ubiquination
negative feedback inhibition

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17
Q

allosteric regulation

A

is a way to activate or inhibit specific enzymes. it happens when effectors bind to specific sites called allosteric sites, on the enzyme, causing the enzyme to change the shape. this can change either activate or inhibit the enzyme, depending on the type of effector.

effectors are small molecules that can bind to an enzyme at a specific location called the allosteric site, and can either activate or inhibit the enzymes activity by causing a change in its shape.

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18
Q

competitive irreversible inhibition

A

competitive Irreversible inhibition is when the inhibitor permanently binds to the enzymes active site and prevents it from functioning, blocks substrate binding.

Competitive irreversible inhibition occurs when an inhibitor irreversibly binds to the active site of an enzyme, preventing the substrate from binding, and permanently inactivating the enzyme.

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19
Q

ubiquitination

A

Ubiquitination is like putting a tag on an enzyme called ubiquitin. This tag tells the cell to get rid of the enzyme by breaking it down into small pieces with special cell machines called proteasomes.

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20
Q

negative feedback inhibition

A

is a type of self-regulation of enzyme-catalyzed processes. product of the reaction can inhibit a prior step in order to prevent over production of a substrate or intermediate. ex regulation of body temperature, blood glucose level. in case of disruption in feedback loop, ex with blood glucose –> overproduction of glucose in blood —> diabetes.

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21
Q

negative feedback inhibition

A

Negative feedback inhibition is a way that enzymes control themselves. The product of a reaction can stop an earlier step to avoid making too much of something. This helps regulate things like body temperature and blood sugar. If the feedback loop is broken, like in the case of too much glucose in the blood, it can cause problems like diabetes.

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22
Q

action mechanism of amylase

A

Amylase’s action mechanism is influenced by pH and temperature. It works best at around 38°C. If it gets too hot, the enzyme changes its shape and becomes denatured, losing its ability to function properly. On the other hand, if it gets too cold, the enzyme slows down, and the substrate takes longer to bind to the active site.

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23
Q

what is bile?

A

Bile is a substance that helps digest fats in our body. It is produced in the liver.

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24
Q

where is bile stored?

A

in the gallbladder

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25
Q

where is bile released?

A

Bile is released from the gallbladder. When food is present in the duodenum, a signaling molecule called CCK is released, which triggers the release of bile.

it is released into the small intestine, specifically in the duodenum

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26
Q

functions of bile

A
  1. Bile helps the body get rid of waste products like bilirubin, cholesterol, steroids, heavy metals, drugs, drug metabolites, and toxins.
  2. Bile helps in the digestion process by breaking down and absorbing food.
  3. Bile helps with the absorption of fats by forming micelles, which are like little carriers that transport fats for absorption in the gut.
  4. Bile salts have powerful properties that can fight against harmful microorganisms in the intestine, protecting the body from infections. They also help maintain a healthy balance of microorganisms in the gut.
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27
Q

composition of bile

A
  • water (80-97%)
  • organic/inorganic components (3-20%) => bilirubin, biliverdin & fats
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28
Q

pH of bile

A

depending on the concentration of bile salts the pH can increase up to 8 but since it mostly consist of water the pH is around 7.

29
Q

primary and secondary bile

A

primary:
synthesized in liver from cholesterol and forms hydroxylated (containing an OH group9 & conjugated (amino acids is added) bile
- can form primary salts
- constitutes 5% of the released bile

secondary:
- gained after bacterial interaction with primary bile salt, produced in colon
- missing OH-group
- constitutes to 95% of the released bile

30
Q

bile acids vs bile salt

A

bile acid = protonated form
bile salt = deprotonated/ionized form
bile salt is formed out of bile acid & potassium or sodium

31
Q

mixed micelles formation with bile

A

bile salts in water can form micells (hydrophilic part to the outside and hydrophobic part of the inside –> amphiphatic. increase the solubility of nonpolar molecules (cholesterol & fatty acids). important to make insoluble molecules (phospholipids & monoglycerides) soluble

32
Q

What is Gallstone disease?

A

Gallstone disease occurs when hard stones form in the gallbladder.

33
Q

What is the most common type of gallstone?

A

The most common type of gallstone is yellow-green and made of cholesterol, called cholesterol stones.

34
Q

What are pigment stones?

A

Pigment stones are smaller and darker stones made of bilirubin.

35
Q

What are the two types of gallstones?

A

The two types of gallstones are cholesterol stones and pigment stones.

36
Q

What is cholestasis?

A

Cholestasis is a condition where the liver is unable to produce or secrete bile properly.

37
Q

What is the result of cholestasis?

A

Cholestasis results in a decrease in the flow of bile.

38
Q

What causes cholestasis?

A

Cholestasis can be caused by damage to the liver cells or blockages in the bile ducts.

39
Q

What are the consequences of cholestasis?

A

Cholestasis can lead to a buildup of toxins in the body and other health complications.

40
Q

What happens if the acidic contents of the stomach are not neutralized by bicarbonate?

A

The enzymes released by the pancreas will not work properly.

41
Q

What is the role of bicarbonate in the duodenum?

A

To neutralize the acidic contents of the stomach.

42
Q

Which organ releases enzymes that are affected by the acidity of the duodenum?

A

The pancreas

43
Q

What is pancreatic insufficiency?

A

Pancreatic insufficiency is a condition where the pancreas does not produce enough enzymes needed for lipid digestion.

44
Q

What causes pancreatic insufficiency?

A

Pancreatic insufficiency is caused by a chronic inflammatory disease.

45
Q

What are the consequences of pancreatic insufficiency?

A

The consequences of pancreatic insufficiency include malabsorption and nutrient deficiencies.

46
Q

What is Hartnup disease?

A

Hartnup disease is an absorption disorder of amino acids where the body has difficulty absorbing normal and basic amino acids in the small intestine and renal tubule.

47
Q

What are the symptoms of Hartnup disease?

A

Hartnup disease can cause symptoms similar to skin pellagra cerebellar ataxia and psychiatric abnormalities.

48
Q

What is cystinuria?

A

Cystinuria is a disorder where the body is unable to absorb an amino acid called cystine properly from the small intestine and renal tubule.

49
Q

What is the main symptom of cystinuria?

A

The main symptom of cystinuria is the formation of kidney stones, which are hard masses made up of crystals that can cause pain and discomfort.

50
Q

What is the main idea of metabolic pathway regulation?

A

The main idea is to regulate the flow of intermediate molecules and metabolites in the pathway to maintain cellular homeostasis.

51
Q

What are metabolites?

A

Metabolites are all molecules that act in the metabolic pathway.

52
Q

What is the difference between catabolic and anabolic pathways?

A

Catabolic pathways produce energy and substrate usually are larger molecules than products, while anabolic pathways consume energy, substrates usually are smaller molecules than products, and produce new molecules.

53
Q

What are the different ways in which metabolic pathways can be regulated inside the cell?

A

Metabolic pathways can be regulated inside the cell by substrate availability, enzyme activity regulation (covalent, allosteric), and changes in key enzyme amount.

54
Q

How can metabolic pathways be regulated outside the cell?

A

Metabolic pathways can be regulated outside the cell by signals from external factors, such as hormones, which can regulate substrate availability.

55
Q

What are regulated enzymes in metabolic pathways?

A

Regulated enzymes are important parts of metabolic pathways that have a specific job to do.

56
Q

At what points in the pathway do regulated enzymes often work?

A

Regulated enzymes often work at points in the pathway where the substrate (starting material) and products (end materials) are the same, but the enzyme is different.

57
Q

What is the first step in a pathway that can’t be reversed called?

A

The first step in a pathway that can’t be reversed is called a “committed step.”

58
Q

What happens once a molecule goes through a committed step in a pathway?

A

Once a molecule goes through a committed step in a pathway, it is committed to continue down the pathway and can’t turn back.

59
Q

What is the first committed step in glycolysis?

A

The first committed step in glycolysis is when the molecule fructose-6-phosphate is turned into fructose 1,6-biphosphate.

60
Q

What are hydrolases?

A

Hydrolases are special enzymes in the digestive tract that break down food into smaller pieces.

61
Q

What is the job of hydrolases in the digestive tract?

A

The job of hydrolases is to break down big molecules into smaller building blocks.

62
Q

What is enzymatic hydrolysis?

A

Enzymatic hydrolysis is the process of breaking down molecules using enzymes, such as hydrolases, into their smaller building blocks.

63
Q

Give an example of enzymatic hydrolysis.

A

An example of enzymatic hydrolysis is the breakdown of proteins into amino acids in the digestive tract, which allows the body to absorb them.

64
Q

What are endohydrolases?

A

Endohydrolases are enzymes that break down the internal covalent bonds of a substrate, but cannot release monomers.

65
Q

What are exohydrolases?

A

Exohydrolases are enzymes that break down covalent bonds at the ends of a substrate, and release monomers.

66
Q

What are esterases and what do they do in the digestive juices?

A

Esterases are enzymes in the digestive juices that break ester bonds with the help of water.

67
Q

What are glycosidases and what do they do in the digestive juices?

A

Glycosidases are enzymes in the digestive juices that break glycosidic bonds in polysaccharides with the help of water. They have subgroups called endoglycosidases and exoglycosidases.

68
Q

What are peptidases and what do they do in the digestive juices?

A

Peptidases are enzymes in the digestive juices that break peptide bonds in polypeptides with the help of water. They have subgroups called endopeptidases and exopeptidases.

69
Q

What is the role of water in the hydrolysis reactions catalyzed by these digestive enzymes?

A

Water is needed to break the chemical bonds in the molecules being digested by these enzymes. It is a key component in the process of hydrolysis, which is the breakdown of large molecules into smaller ones.