7.2 enzyme pre-vocab Flashcards
learning terms and meanings early ! (also rewrite of in-class notes !)
Collision Theory
In order for reactants to collide, there needs to be the correct setup (sides that will collide and same direction to fit together), and the correct speed for them to LITERALLY slam into each other.
Enzyme Concentration
The higher the concentration of enzymes, the higher the rate of success when the collisions to occur.
The more enzyme = more likely to run into subrate to combine.
Substrate Concentration
More successful reactions with enzymes, but the enzymes can hold take so make substrates at a time, so we see a decrease over time. (Rise, peak, then stay)
Temperature
The higher the temperature, the higher speeds of motions for collisions. If the molecules move faster, there is a higher rate of collison.
(If too hot, enzymes will start to deshape/denature. Also the graph kinda looks like a wee-wee…)
pH
If it’s too basic or too acidic, things will start to fall apart. (aka; protien will start to denature.) pH will affect proteins like temperature. They need the correct pH to function. (and not fall apart!) ((Graph has like 3 wee-wees….)
How would you turn an enzyme, “on?”
By adding an activator to activiate the active sites in order to fit the substrates. (CHANGES SHAPE TO ALLOW)
- cofactors: inorganic ions (ex. zinc, iron, etc.)
- conenzymes: vitamins (ex. a, b, etc.)
How would you turn an enzyme, “off?”
By adding an inhibitor that races/competes with the enzyme in order to change its shape before a substrate can reach it.
What is the difference between competitive and noncompetitve inhibitors?
Competitive inhibitors race the substrates for the active site, and DO NOT allow the substrates to combine with active site.
Noncompetivite inhibitors allow substrates to bind to enzyme first, but after the noncompetitive ones get there, they change the shape of the active site, making the substrate break away.
