Enzymes Flashcards
(24 cards)
Prosthetic group
Type of cofactor that is tightly and permanently bound to an enzyme
Cofactor
Non-protein component that help transfer atoms or groups between reactions or form part of an active site
Where are cofactors obtained from?
Obtained from our diet as minerals (iron, calcium, chloride, zinc ions etc)
Coenzymes
Organic cofactors
Where are coenzymes obtained from?
Obtained from our diet as vitamins (vitamin B3 etc)
Precursor activation via cofactors
Some enzymes are inactive and need a change in their tertiary structure through a cofactor.
apoenzyme + cofactor activator/coeznyme –> holoenzyme
Precursor activation via enzymes
Enzymes can change the tertiary shape of other enzymes to activate them.
zymogen / proenzyme + enzyme –> holoenzyme
give an example of an intacellular and an extracellular enzyme
intracellular - catalase
extracellular - amylase
what do you call enzymes that are activated by either another enzyme or a change in condition?
zymogens or proenzymes
why might precursor enzymes be inactive?
- avoid causing damage to cells or tissues that release or transport them
- enzymes may only be needed under certain conditions
name an intracellular and an extracellular enzyme and what do they break down?
intracellular: catalase breaks down H2O2
extracellular: amylase breaks down starch into maltose
where is amylase secreted?
- salivary glands
- pancreas
can cold temperatures denature enzymes?
no, they can inactivate enzymes but not denature them
Q10
temperature coefficient - measures the change in rate of reaction over a 10°C temperature change
when does Q10 not apply?
once the temperature exceeds its optimum
what is the usual Q10 for enzyme controlled reactions?
2 (rate doubles)
which extremophilic enzymes are more sensitive/less stable to change and why?
- enzymes in psychrophilic organisms (adapted to cold temperatures)
- more flexible enzyme structures specifically at the active site (small changes will denature them)
how do H+ affect enzymes?
- H+ form ionic bonds and H bonds between R groups in enzyme’s tertiary structure
- this also affects the R groups’ interactions with each other
which factors permanently (irreversible) or temporarily (reversible) denature enzymes?
temporarily: pH within limits and low temp
permanently: pH beyond limits and high temp
renaturation
change in conditions returns a reversibly denatured enzyme back to its original, specific shape
how does an acidic pH (beyond optimum) affect enzymes?
- high [H+]
- form ionic and H bonds with R groups
- less R groups can interact with each other
- bonds are broken
- tertiary structure is altered
and vice versa for alkaline conditions (beyond optimum)
Q10 formula
Q10=R2/R1
how does temperature affect membrane permeability?
- increase temp, increases KE
- phospholipids move more freely
- membrane more fluid therefore more permeable
- AND proteins may denature, leaving gaps in membrane
how do solvents affect membrane permeability?
- solvents like ethanol (non-polar alkyl chain and polar OH group) interact with the phospholipids
- solvents dissolves/surrounds phospholipids
- more bigger gaps in membrane increases permeability