Master this deck with 25 terms through effective study methods.
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Cofactors and coenzymes
a non protein part of the enzyme that some enzymes require to be active. It can be either organic or inorganic
an organic cofactor which is made from vitamins like B3
Inhibitors
Competitive and non-competitive inhibitors
Allosteric site
Non competitive inhibitors alter the active site so the enzyme is non functional no matter how many substrates there are. Whereas competitive inhibitors just get diluted out by increasing substrate concentration
the term used for enzyme inhibition that occurs when the product of a reaction acts as an inhibitor to the enzyme that produces it
It is toxic and causes damage to cells
It is naturally produced as a biproduct of aerobic respiration
2
When enzymes are produced in an enzyme inactive form also known as an apoenzyme
Through a cofactor or coenzyme which changes the shape of the active site to make it complememtary
When a precursor enzymes becomes activated by temperature or ph changing their active site
Holoenzyme
protein digesting enzyme produced by the pancreas
Lock and key model and induced-fit hypothesis
the shape of the enzyme changes when the substrate fits into the active site because the initial binding is weak and the binding can weaken bonds within the reactants
Extracellular enzymes
They secrete enzyme into their immediate environment and then they absorb the smaller molecules
More number of bonds in their tertiary structure like sulphide bridges and hydrogen bonds which makes them more stable. Resistant to temperature change
They are more flexible , making them less stable an smaller temperature changes denature them
Renaturation
A change In hydrogen ion concentration affects how much the ions interact with the polar or charged R groups on amino acids and changes how much they interact with each other
Prosthetic groups bind strongly and permanently form a part of the protein