week 6 - keywords

Question 1

proteolytic inhibition

Answer 1

is a process where enzymes called proteases that break down proteins are stopped/blocked from doing their job. It can happen naturally in the body or by drugs. proteolytic inhibition prevents the breaking down of proteins into smaller parts by inhibiting the activity of proteases (enzymes).

Question 2

allosteric regulation

Answer 2

is a process where a molecule called allosteric regulator binds to an enzyme and either decreases or increases the activity of an enzyme. so the allosteric regulator can either be an inhibitor or an activator. If the activator binds to the enzyme it will increase the activity but if an inhibitor binds to the enzyme it will decrease the activity. the binding of the allosteric regulator does not occur at the active site, it occurs at a different place.

Question 3

mixed inhibition

Answer 3

mixed inhibtion is a type of enzyme inhibtion where the inhibitor can bind to both the enzyme and the enzyme-substrate complex at different site (på olika ställen). This type of inhibition results in a decrease in the rate of the enzyme reaction, and the degree of inhibition depends on the concentration of both the substrate and the inhibitor. Mixed inhibition is different from competitive inhibition and non-competitive inhibition, as it can affect both the binding of the substrate and the catalytic activity of the enzyme.

Question 4

competitive inhibtion

Answer 4

• Competitive inhibition occurs when a molecule similar in shape to the substrate binds to the active site of an enzyme and prevents the substrate from binding.
• This is like when someone else takes your seat on a bus or a train, so you can’t sit there anymore.
• The inhibitor and substrate compete for the same spot on the enzyme, and the more inhibitor present, the less substrate can bind.
• This reduces the enzyme’s activity, slowing down the reaction it catalyzes.

Question 5

covalent modification

Answer 5

• can be reversible or irreversible
• can include processes such as phosphorylation, methylation, and glycosylation
• Covalent modification is a process where a molecule, like a protein or nucleic acid, can be changed chemically by making a new bond with another molecule.
• This change can affect the molecule’s function or activity, making it more or less active or changing how it interacts with other molecules in the body.
• Examples of covalent modifications include adding or removing chemical groups like phosphate, methyl, or sugar groups.
• These modifications are important because they help regulate how molecules work in the body.

Question 6

proteolytic cleavage

Answer 6

Proteolytic cleavage is a process where a protease enzyme cuts a protein into smaller pieces by breaking the peptide bonds between amino acids.

• This is similar to cutting a long piece of paper into smaller pieces using scissors.
• Proteolytic cleavage plays a crucial role in many biological processes, such as protein activation, regulation, and degradation.
• When a protein is cleaved, it can change its function or become inactive.
• Additionally, proteolytic cleavage can produce new proteins with unique functions.

Question 7

Uncompetitive inhibition

Answer 7

• Uncompetitive inhibition is a type of enzyme inhibition.
• In this process, an inhibitor molecule binds to the enzyme only after the enzyme has bound to its substrate.
• The inhibitor then locks the enzyme-substrate complex in a way that prevents the release of the reaction product.
• This slows down the reaction and reduces the enzyme’s activity.
• The inhibitor cannot bind to the free enzyme, only to the enzyme-substrate complex.
• This type of inhibition is non-competitive with the substrate, meaning that the inhibitor binds to a different site on the enzyme.