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.
Products:
Glucosex
  Reactants: Maltose 2

Enzyme
Substrate substrate
Reaction=Hydrolysis
complex
; results in water
Active Site

Enzyme Induced Fit/ Correct Enzyme reused

Allosteric Site orientation
(Enzyme On) OH - - - H
Hydrogen Bond (Change in protein
shape)-Enzyme off
Increase in temp.

Denaturation;
change in protein
shape Feedback inhibition

2. Explain why the environment of an enzyme is so important for the functionality of an enzyme.
The environment of an enzyme is so important for the functionality of an enzyme because the factors in the
environment; such as drastic change in pH or temperature can break the bonds in the secondary or tertiary
structure of the enzyme. When these bonds break the enzyme will not be the same shape, meaning the substrate
will no longer be able to fit into the enzyme affecting the functionality.
Explain 2 ways how an enzyme can be inhibited.

Enzymes can be inhibited with a competitive inhibitor; which is a molecule that blocks the active site of an enzyme
meaning the substrate cannot attach to the enzyme. They can also be inhibited with a non-competitive inhibitor; this is a
molecule that attaches to the allosteric site of an enzyme which then changes the shape of the active site, prohibiting the
substrate from then attaching to it.

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)

3. 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.

mutation 1: Ser, Tyr, Asn, Thr

mutation 2: Ser, Ala, Asn, Thr

Mutation 2 would have a more detrimental effect because in the original sequence, all the molecules are polar,
meaning they would be attracted to each other. However, Tyr is also a polar molecule, meaning it will likely
resemble close to the original sequence. However, Ala is a nonpolar molecule, meaning that there would most
likely be a change in folds since the molecule will not be attracted to the rest of the molecules. The remaining
molecules will likely surround the nonpolar molecule because they are attracted to each other and not the
nonpolar molecule, and surrounding the nonpolar molecule maximizes the surface area. This would probably
change the folding of the enzyme and have an effect on the active site shape.