AP BIO ENZYMEE QUIZ

Enzymes:

Enzymes:

are biological catalysts, typically proteins (although RNA molecules called ribozymes also exhibit catalytic activity), that accelerate the rate of chemical reactions in living organisms by lowering the activation energy required for the reaction to proceed. They remain unchanged and reusable after the reaction.

Catalyze

• speed up reactions by lowering activation energy (Not used up/reusable)

• tertiary structure must be maintained to maintain function.

Active Site

Enzyme uses substrates through this. It has a unique shape, physical and chemical properties must be compatible, and slight changed can occur in order to bind with a substrate.

Synthesis and Hydrolysis

These are Digestive Reactions that Enzymes play a big role in. Ex. Breaks down proteins, carbohydrates, nucleic acids into simpler substances for energy. Helps boost metabolism

Activation Energy

Is how Enzymes are able to function. Some absorb energy, some release. (reactions releasing require less energy than absorbing). Enzymes can lower this in order to gain a faster reaction.

Controlled Experiment

is designed to test a hypothesis by comparing an experimental group exposed to a specific treatment or manipulation with a control group that remains unchanged. This allows researchers to isolate the effect of the independent variable (the treatment) and minimize the influence of other variables.

Control Group

are experimental conditions that do not receive the treatment or manipulation being tested. They provide a baseline for comparison with the experimental group, helping researchers determine whether observed effects are due to the treatment or other factors.

Negative Controls

Not exposed to any treatment

Positive Controls

exposed to treatment with a known effect. Not exposed to the Experiment treatment

Experimental Group:

is the group subjected to the treatment or manipulation being tested. Data collected from this is compared with data from the control group to assess the effects of the treatment.

Controlled Variables:

are factors intentionally kept constant in an experiment to isolate the effect of the independent variable

Denaturation

•  changes in the conformational shape of the enzyme and can be caused by changes to their environment

  • Temperature change

  • pH change

  •  typically irreversible leading to decrease/loss of enzyme activity In some cases it can be reversible and enzyme activity it regained

Optimum Temperature

 range where enzyme-mediated reactions occur fastest. If not maintained results in change in reaction rates

Increased temp. for Enzymes

• Initially increases reaction rate

  • Increased speed of molecular movement

  • Increased enzyme-substrate collisions

• When increased outside optimum range results in denaturation

Decreased Temp in Enzymes

• Generally slows down reactions

  • Decreased enzyme-substrate collisions

  • Does NOT disrupt structure, no denaturation

PH

• measure hydrogen ion concentration in solutions

  • (-log[H+])

  • Small changes in this lead to large shifts in ion concentration

Optimum pH

Range in which enzyme - mediated reactions occur fastest. PH outside the range will slow or stop the reaction

• Increase and decrease in pH outside this range will denature enzyme

• Changes in H+ concentration can disrupt hydrogen bond interactions that help maintain enzyme structure.

Substrate concentration

• Initial increases in this concentration increases reaction rate

  • More of this means more opportunity to collide with enzyme

  • This saturation will eventually occur results in no further increase in rate

  • Reaction rate will remain constant if these levels are maintained

Product Concentration

decreases opportunity for addition of substrates. More matter takes up space, more product in the area means lower chance of substrate - enzyme collisions. SLOWS REACTION

Enzyme Concentration

Less = slower reaction rate. Less opportunity for substrates to collide with active sites

More= faster reaction rate. More opportunity for substrates to collide with active sites

Competitive Inhibitors:

are molecules that closely resemble the substrate and compete with it for binding to the active site of the enzyme. They do not undergo the catalytic reaction but instead block the active site, preventing the substrate from binding and reducing the rate of enzyme activity. Can be overcome by increasing the substrate concentration.

Noncompetitive Inhibitors:

bind to sites on the enzyme other than the active site, known as allosteric sites. Binding of a this inhibitor induces a conformational change in the enzyme that reduces its catalytic activity, even in the presence of the substrate. This inhibition cannot be overcome by increasing the substrate concentration.