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- typically proteins
- speed up the rate of reaction within the cell by lowering the amount of activation energy necessary (catalyst)
- may break large molecules into smaller molecules, or bind molecules together

Substrates:
- molecules that the enzyme binds to
- the active site is the location where the enzyme binds to the substrate

Interaction Theories:
Lock and Key Theory
- the active site of the enzyme is precisely shaped to hold the specific    substrate
Induced Fit Theory
- the active site and the substrate don't fit perfectly together, but alter their shape to connect(LOCK AND KEY THEORY DIAGRAM)

(INDUCED FIT THEORY DIAGRAM)

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Optimal Conditions include:
- Temperature
The ideal temperature for enzymes in the human body is approximately 35 - 40 degrees Celsius. Once the ideal temperature for maximum rate of reaction is achieved, this is called the Optimum Temperature.
- pH Value
The optimal pH range for most enzymes are 6 and 8.
- Substance Concentration
The higher concentration an enzyme solution is, the faster it will be able to preform chemical reactions in the body. However, once an enzyme has reached it's maximum rate of reaction, it will no longer speed up even if you make the solution more concentrated.

This video explains it well:
https://www.youtube.com/watch?v=D2j2KGwJXJc

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- Substances that attach to a binding site on an enzyme other than the active site, causing a change in the enzyme shape and a loss of affinity for its substrate
- All noncompetitive inhibition is allosteric, but not all allosteric inhibition is noncompetitive inhibition.  Allosteric can be competitive and non-competitive.

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https://padlet.com/tylewill861/3vydavihaj6m

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Cells tightly regulate their enzymatic reactions, allowing necessary reactions to proceed while inhibiting unnecessary or damaging ones. One means of regulating enzyme action is allosteric regulation. Enzymes speed up chemical reactions, making reactions occur at the right time and place in a cell.Allosteric regulation occurs when a non-substrate molecule binds or modifies a site other than the active site of an enzyme (called the allosteric site), thereby inducing the enzyme to change its shape. The shape change can result in the activation or inactivation of an enzyme.

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-"a cellular control mechanism in which a cell's activity is inhibited by the enzymes end product"

-the end product of the reaction returns to a specific site to halt production
-prevents from too much of the product being made
-balances production of amino acids, the building blocks of proteins
-necessary to prevent enzymes from breaking down too many molecules that are energy sources for the cell, such as glucose

-inhibition takes place in glycolysis, the process of breaking down the sugar glucose to produce the cell's "energy currency" molecule ATP
-ATP slows down the enzymes until they're structurally modified and stops catalyzing reactions, the enzymes are inhibited when blood glucose levels are low, so there isn't a total depletion and the cell then has a chance to accumulate more glucose for later use