sammanfattning på allt viktigt Flashcards
enzymes
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.
simple enzymes
do not need help by non-protein components to fulfill its job
complex enzymes
need non-protein components like cofactors (inorganic compound) or coenzymes (organic compound)
is cofactor an organic or inorganic compound?
inorganic compound
is coenzyme an organic or inorganic compound?
organic compound
is it true that enzyme that needs cofactor is not functional without it?
yes
apoenzyme
enzyme without cofactor or prosthetic group but has a coenzyme. when it binds to an coenzyme it becomes active apoenzyme
holoenzyme
enzyme with cofactor and/or prosthetic group
carboxylation
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.
enzyme acitivty
refers to how well enzyme can do its job which is to speed up chemical reactions in the body
name the specific enzyme activations:
- allosteric regulation
- proteolytic cleavage
- covalent modification
What is reversible competitive inhibition and how does it affect the efficiency of an enzyme?
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.
covalent modification
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.
zymogen
is an inactive form of an enzyme that requires a biochemical change to become active.
proteolytic cleavage
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.
name all the different specific enzyme inhibtions
reversible competitive inhibition
allosteric inhibition
uncompetitive inhibition
mixed inhibition
irreversible competitive inhibtion
ubiquination
negative feedback inhibition
allosteric regulation
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.
competitive irreversible inhibition
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.
ubiquitination
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.
negative feedback inhibition
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.
negative feedback inhibition
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.
action mechanism of amylase
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.
what is bile?
Bile is a substance that helps digest fats in our body. It is produced in the liver.
where is bile stored?
in the gallbladder
where is bile released?
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
functions of bile
- Bile helps the body get rid of waste products like bilirubin, cholesterol, steroids, heavy metals, drugs, drug metabolites, and toxins.
- Bile helps in the digestion process by breaking down and absorbing food.
- Bile helps with the absorption of fats by forming micelles, which are like little carriers that transport fats for absorption in the gut.
- 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.
composition of bile
- water (80-97%)
- organic/inorganic components (3-20%) => bilirubin, biliverdin & fats