Group 3
Group 3
Group 3
Enzyme Regulation
Enzymes
-are naturally-produced proteins that act as biological catalysts, meaning that they help speed
up chemical reactions in organisms' bodies. This process is achieved by the binding of enzymes
to substrates, the complex molecules that enter cells and upon which enzymes act. Each
enzyme type has specific substrates to which they can bind. After binding, enzymes break the
substrates down into smaller products that can be processed by the organism's body into
energy. All enzymes should not be activated at the same time or in the same cell; instead,
enzyme regulation should occur. Enzyme regulation is a careful control system of enzymes in
which some enzymes are turned on while others are turned off.
Enzyme and substrate bind forming an enzyme-substrate complex and the enzyme breaks down
the substrate
There are certain factors that help regulate enzymes that include genetic enzyme regulation,
compartmentalization, substrate concentration, degradation of enzymes, alteration of
environmental factors, modification of zymogens, covalent modification, allosteric regulation,
and inhibition.
Genetic Regulation
Genetic regulation is one of the many mechanisms that regulate enzymatic activity. It is
achieved by regulating how many enzymes are produced by the organism's body. If the body
needs more enzymes to be produced, then induction of the gene producing the enzyme takes
place. On the other hand, if the body need fewer enzymes to be produced, then the gene
producing the enzyme is repressed.
Compartmentalization
Enzymes are also regulated by compartmentalization, which mostly occurs in eukaryotic cells.
During compartmentalization, enzymes are separated by cellular membranes that restrict their
movement to a certain "compartment" (usually a cell organelle). This means that such enzymes
are only able to function inside the compartment and will not be able to reach substrates
outside of the compartment. This method of regulation can also provide the right environment
for enzymatic activity to occur.
An example of this type of enzymatic regulation can be found in the enzymes localized to
lysosomes, organelles that help break down cellular material. Another example is the enzymes
localized to mitochondria, which can reach an extreme internal environment compared to the
rest of the cell. These conditions (a relatively-higher temperature and pH) allow the functions
of certain enzymes to be enhanced.
Substrate Concentration
Substrate concentration is another method for enzyme regulation during which the number of
substrates available is controlled. If substrates are not readily available for enzymes to bind and
break them down, then enzymes will not be activated, even though there may be many
enzymes available.
Degradation of Enzymes
Enzymatic degradation also regulates the number of enzymes available to bind to and break
down substrates. Degradation of enzymes occurs by breaking down enzymes themselves;
however, substrates can also be degraded.
Enzyme activity can also be regulated through the alteration of environmental factors. There
are certain environments in which enzymes function at their best. In particular, enzymes have
specific temperature and pH ranges that facilitate their activity. With this in mind, enzyme
regulation takes place by changing the temperature or pH level, thus effecting enzymatic
function.
Modification of Zymogens
Zymogens (also called proenzymes) are inactive enzymes that can become active enzymes.
However, zymogens need a chemical modification (oftentimes by other enzymes) to be
activated. A control mechanism at the level of chemical modification of zymogens manages the
production of activated enzymes.
Covalent Modification
Some enzymes are regulated by covalent modification, a mechanism that involves covalent
binding of a singular molecular group. Through this method, enzyme regulation takes place by
addition or subtraction of the molecular group.
Allosteric Regulation
Allosteric regulation is also a common means to control enzymatic activity. Through what is
allosteric regulation achieved? Regulatory molecules, activator molecules that "turn on" or
inhibitor molecules that "turn off" enzymes, bind to an enzyme's allosteric site, a site where
molecules can bind to and change the shape and consequently, its function. Changing the
shape of the enzyme affects the shape of its active site, the site where enzymes bind to their
substrates. If the shape of the enzyme's active site and the substrate do not match, then they
cannot bind to each other and the substrate is not broken down. Note that a change in shape
could also lead to an enhancement of enzymatic-substrate affinity thus, increasing the number
of substrates that are broken down.
Cooperativity
Allosteric proteins show the property of cooperativity i.e., activity at one functional site affects
the activity at others. A slight change in substrate concentration can produce substantial
changes in activity. Their kinetics do not obey the Michaelis-Menten equation. Their V versus
[S] plots yield sigmoid curves rather than hyperbolas.
Positive cooperativity: Ligand binding at one site facilitates the binding of other sites on
the same molecule.
Negative cooperativity: Ligand binding at one site inhibits the binding of other sites on
the same molecule.
Regulatory enzymes for which substrate and modulators are identical are called Homotropic.
When the modulator is a molecule other than the substrate, the enzyme is said to be
Heterotopic.
Isoenzymes are enzymes that differ in amino acid sequence yet catalyze the same reaction.
Zymogens or proenzymes acquire full activity only upon specific proteolytic cleavage of one
or several of their peptide bond. Irreversible process.
The covalent attachment of a molecule can modify the activity of enzymes and many other
proteins. A donor molecule provides a functional moiety that modifies the properties of the
enzyme. Most modifications are reversible.