You are on page 1of 1

Name: GUTIERREZ, Mikaela Rose Enzyme Biochemistry Lecture

3C - Biochemistry 1st Shifting Quiz #1 (Intro to Enzymes)

ANSWER BRIEFLY. MAX OF 5 SENTENCES PER ITEM

1. Describe how an enzyme accelerate rate of reaction.


Enzymes are biological catalysts. Catalysts are known for lowering their activation energy for reactions, activation
energy is needed to start a chemical reaction. The lower the activation energy for the reaction, the faster the rate. Enzymes
accelerate reactions by lowering activation energy.

2. Like a chemical catalyst, an enzyme is efficient (or even better) in speeding up rate of reaction without
affecting equilibrium concentration of reactant/product. Both are also recycled after the reaction. Give at
least one advantage of using enzyme over a chemical catalyst.
Enzymes are involved in life process. Since enzymes are larger than chemical catalysts, there are more contact points
between the enzyme and substrates wherein enzymes can function in milder conditions meaning the new formed
molecules does not need protection during the reaction. Because of this, modification can also be made to the enzyme
through protein engineering, so it can bind with different substrate.

3. Give at least one feature of an active site and describe briefly


Each subunit of an enzyme has one active site that is capable of binding to substrates. The active site is composed of
aminod acid residues that form bonds with the substrate. It has different important roles in catalysis, substrate binding,
and stabilization of structure during reaction. It also provide suitable environment for the catalysis so that the substrate
can form contact points for strong binding.

4. The active site confers to specificity of an enzyme. What is the difference between geometric and electronic
complementarities of active site (on an enzyme) to substrate?
In geometrical specificity, the substrate binding site has indentation or cleft on the surface of an enzyme. The cleft is
complementary in shape to the substrate. In electronic complementarity, the amino acid residues forms the binding site
specifically to attract the substrate.

5. Identify the two models of active site and describe each briefly
There are two models used to describe the active site: (1) Lock and key model, it proposed that the lock symbolizes
the enzyme, the key is the substrate, while the keyhole is the active site. The appropriate size of the key will only fit the
keyhole of the lock. (2) induced fit model, it proposed that the enzyme's active site is flexible that it changes its shape so
that the substrate will fit.

You might also like