8.2- Enzymes Flashcards
What are the 11 general characteristics of enzymes?
1) Biological catalysts
2) Effective in small amounts
3) Act on specific substrates to generate specific products
4) Increase the rate of a reaction
5) Provide route from reactants to products that has a lower activation energy
6) Not consumed or permanently changed in a reaction
7) Can be regulated to control biochemical pathways
8) Some require cofactors to be active
9) Genetically determined
10) Often names after its substrate and/or the type of reaction it performs
11) Name often ends in “asa”
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Define collision theory
Energy transferred during collisions between atoms and molecules can disturb the electron structures of atoms and molecules enough to make or break chemical bonds.
Define substrate
The molecule that an enzyme acts on.
Define active site
The site where the enzyme and substrate interact
Define induced fit model
The way that enzymes and substrates are thought to interact- the enzyme can mold slightly to the substrate to encourage the chemical reaction desired.
Define transition state
Brief period when reactants are chemically becoming products, but the reaction isn’t complete.
Define cofactors
Additional components that some enzymes need to function.
Apoenzyme
An enzyme that is inactive because it doesn’t have ti’s cofactors.
Holoenzyme
Functional form of enzyme where the enzyme has the cofactors that it need to function.
Coenzymes
Organic cofactors
Allosteric regulation
Non-permanent regulation of an enzyme through biding to the allosteric inhibitor or activator. Acts as a volume control for the productivity or lack of productivity caused by an enzyme.
Define feedback inhibition
Slows down or turns off biochemical pathways. Works like a thermostat- turning on when something the enzyme helps encourage through biochemical pathways is needed, and turns off when the “end product” is not needed, or there is enough of it.
Define competitive inhibition
These slow enzyme reactions by competing with substrates for the target enzymes active site. This can be overcome if the concentration of substrates is greater than the concentration of competitors.
Define non-competitive inhibition
Non-Competitive inhibitors don’t compete to control an enzymes active site. They bind to sites other than active sites. The non-competitive inhibits usually distort the natural shape of the enzyme.
