1. What factors influence the activity of enzymes?

 The six factors are: (1) Concentration of Enzyme (2) Concentration of Substrate (3)
Effect of Temperature (4) Effect of pH (5) Effect of Product Concentration and (6) Effect
of Activators.

2. How do enzymes work? Describe the different mechanisms involved

 Enzymes are biological molecules (typically proteins) that significantly speed up the rate
of virtually all of the chemical reactions that take place within cells.
 They are vital for life and serve a wide range of important functions in the body, such as
aiding in digestion and metabolism.
 Some enzymes help break large molecules into smaller pieces that are more easily
absorbed by the body. Other enzymes help bind two molecules together to produce a new
molecule. Enzymes are highly selective catalysts, meaning that each enzyme only speeds
up a specific reaction. [What Is Chemistry?]
 The molecules that an enzyme works with are called substrates. The substrates bind to a
region on the enzyme called the active site.
 There are two theories explaining the enzyme-substrate interaction.
 In the lock-and-key model, the active site of an enzyme is precisely shaped to hold
specific substrates. In the induced-fit model, the active site and substrate don't fit
perfectly together; instead, they both alter their shape to connect.
 Whatever the case, the reactions that occur accelerate greatly — over a millionfold —
once the substrates bind to the active site of the enzyme. The chemical reactions result in
a new product or molecule that then separates from the enzyme, which goes on to
catalyze other reactions.
 Here's an example: When the salivary enzyme amylase binds to a starch, it catalyzes
hydrolysis (the breakdown of a compound due to a reaction with water), resulting in
maltose, or malt sugar.
 The mechanism of enzymatic action. An enzyme attracts substrates to its active site,
catalyzes the chemical reaction by which products are formed, and then allows the
products to dissociate (separate from the enzyme surface). The combination formed by
an enzyme and its substrates is called the enzyme–substrate complex.

3. How are enzymes regulated?

 Enzymes can be regulated by other molecules that either increase or reduce their activity.
Molecules that increase the activity of an enzyme are called activators, while molecules
that decrease the activity of an enzyme are called inhibitors.
 The cell uses specific molecules to regulate enzymes in order to promote or inhibit
certain chemical reactions. Sometimes it is necessary to inhibit an enzyme to reduce a
reaction rate, and there is more than one way for this inhibition to occur.
  In competitive inhibition, an inhibitor molecule is similar enough to a substrate that
it can bind to the enzyme’s active site to stop it from binding to the substrate. It
“competes” with the substrate to bind to the enzyme.
 In noncompetitive inhibition, an inhibitor molecule binds to the enzyme at a
location other than the active site (an allosteric site). The substrate can still bind to
the enzyme, but the inhibitor changes the shape of the enzyme so it is no longer in
optimal position to catalyze the reaction.

4. Lactate dehydrogenase’s optimal temperature is 36°C. It is irreversibly inactivated

at 85°C but yeast containing this enzyme can survive for months at -10°C. How?

5. How are enzymes used in the field of medicine? Give 3 specific examples

EC
Enzyme Reaction Use
number
Asparaginase 3.5.1.1 L-Asparagine H2O L-aspartate + NH3 Leukemia
Collagenase 3.4.24.3 Collagen hydrolysis Skin ulcers
Glutaminase 3.5.1.2 L-Glutamine H2O L-glutamate + NH3 Leukemia
Hyaluronidase a 3.2.1.35 Hyaluronate hydrolysis Heart attack
Lysozyme 3.2.1.17 Bacterial cell wall hydrolysis Antibiotic
Cyanide
Rhodanase b 2.8.1.1 S2O32- + CN- SO32- + SCN-
poisoning
Ribonuclease 3.1.26.4 RNA hydrolysis Antiviral
Penicillin
b-Lactamase 3.5.2.6 Penicillin penicilloate
allergy
Streptokinase c 3.4.22.10 Plasminogen plasmin Blood clots
Trypsin 3.4.21.4 Protein hydrolysis Inflammation
Uricase d 1.7.3.3 Urate + O2 allantoin Gout
Urokinase e 3.4.21.31 Plasminogen plasmin Blood clots

Sources:

http://www1.lsbu.ac.uk/water/enztech/medical.html
https://courses.lumenlearning.com/boundless-biology/chapter/enzymes/
https://www.khanacademy.org/science/biology/energy-and-enzymes/enzyme-
regulation/a/enzyme-regulation
http://www.biologydiscussion.com/enzymes/factors-affecting-enzyme-activity-6-factors/11207
https://www.livescience.com/45145-how-do-enzymes-work.html