HW Proteins/Enzymes

Find a model and label all these parts :

1. Enzyme, active site, enzyme- substrate complex, hydrogen bond, induced fit, correct orientation, substrate,
reactant, products, hydrolysis, water, maltose, glucose x2, feedback inhibition, off, on, allosteric site, reused,
denaturation, increase in temperature, protein shape.
Reactant

Hydrogen Hydrolysis

Induced Fit
Correct Orientation

Protein Shape

Increase in Temperature

2. Explain why the environment of an enzyme is so important for the functionality of an enzyme.
- Each enzyme works better under some conditions than other conditions, because these optimal condidions
favor the most active shape for the enzyme, For example, temperature and pH are environmental factors that
important in the activity of an enzyme. If the temperature too high, the bonds will be disturbed, leading to the
denaturization of the enzyme.

3. Explain 2 ways how an enzyme can be inhibited.

a. Competitive Inhibitors: The reduce the productivity of enzymes by blocking substances from entering active
sites by mimicking the substrate.
b. Non-competitive inhibitors: It binds to the enzyme away from the active site, altering the chape of the enzyme
so that even if the substrate can bind, the active site functions less effectively, if at all.
 The following is an (admittedly terrible) representation of an enzyme protein folded into its proper 3-D
conformation. Go to the amino acid sheet from the textbook so you can see all the amino acids to answer some of
the questions below.

active site (involves amino acids 212,

213, 240, 242)

non-binding region (involves amino

allosteric site acids 304 - 307)
(involves amino acids
406, 407, 415, 417)

4. Let’s say that the proper amino acid sequence for the active site region (AAs 212, 213, 240 and 242) are the
following: Ser, Gln, Asn, Thr

A DNA mutation occurs that changes one of these amino acids – which change below will have a more detrimental
effect on the active site shape (and thus negatively affect its ability to bind to the proper substrate chemical)? Justify
your answer.
I think that mutation 2 will have a more detrimental effect on the
mutation 1: Ser, Tyr, Asn, Thr active site shape because the amino acid that is replacing
Glutamine is Alanine. Alanine is hydrophobic and has nonpolar
mutation 2: Ser, Ala, Asn, Thr
side chains while the amino acid in mutation 1 is Tyrosine,
which is a hydrophilic amino acid and has polar side chains. The
original amino acid sequence had all hydrophilic amino acids as
well so Alanine will probably change the active site shape more.