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Enzymes and Biomolecules

Total questions: 25

Worksheet time: 13mins

Name
Class
Date
1.

An (a)   is a special type of catalyst that is made by a living organism. We sometimes call them biological catalysts. 

2.

What is the name of the special region of an enzyme that binds to the substrate? 

a)

Active area

b)

Unique site

c)

Complementary region

d)

Active site

3.

Any substance that is acted upon by an enzyme is called a:

a)

Coenzyme

b)

Substrate

c)

Vitamin

d)

Polypeptide

4.
After the enzyme and substrate bind together and perform the reaction, what does the substrate become?
a)
a substrate
b)
an enzyme
c)
a product
d)
an active site
5.

Pancreatic amylase is a digestive enzyme found in the small intestine. It helps break down large starch molecules later in the digestive process. Pancreatic amylase is unable to break down proteins.

Which of the following best explains why pancreatic amylase is able to break down starches, but not proteins?

a)

Enzymes are specific to their substrates

b)

Proteins are too large to be affected by enzymes

c)

Enzymes and proteins cannot break down other proteins

d)

Proteins are able to easily denture enzymes

6.

At first, scientists thought that in order for an enzyme to catalyse a reaction, the substrate had to fit perfectly into the active site.

What was the name for this model of enzyme action?

a)

The original model

b)

The lock and key model

c)

The induced fit model

d)

The induced key model

7.

We now know that in order for an enzyme to catalyse a reaction, the enzymes active site actually changes shape slightly as it binds to the substrate.

What do we call this model of enzyme action?

a)

The new model

b)

The lock and key model

c)

The induced fit model

d)

The induced key model

8.

An enzyme speeds up a reaction by:

a)

lowering the activation energy

b)

raising the activation energy

c)

releasing energy

d)

absorbing energy

9.
Which of the following conclusions can be drawn from this graph?
a)
The optimum pH of the enzyme is 6.6.
b)
The optimum pH of the enzyme is 5.8
c)
The enzyme’s activity increases as pH increases 5.0 to 9.0
d)
The enzyme’s activity is greater around pH of 8.0 .
10.

What effect does high temperature have on enzymes?

a)

Denatures them

b)

Inactivates them

c)

Destroys them

11.
What are the four biological molecules?
a)
proteins, carbohydrates, lipids, nucleic acids
b)
A, T, C, G
c)
water, air, earth, and fire
d)

oxygen, water, carbon, nitrogen

12.

What does organic mean (in chemistry)?

a)

It costs more at the grocery store

b)

It contains carbon and hydrogen

c)

It is made of many individual parts

d)

It produces energy

13.

What is the monomer that makes up carbohydrates?

a)

Monosaccarides

b)

Fatty Acids

c)

Amino Acids

d)

Nucleotides

14.

What are triglycerides made of?

a)

Monosaccarides

b)

Fatty Acids

c)

Amino Acids

d)

Nucleotides

15.

What is the monomer that makes up proteins?

a)

Monosaccarides

b)

Fatty Acids

c)

Amino Acids

d)

Nucleotides

16.

What is the monomer that make up nucleic acids?

a)

Monosaccarides

b)

Fatty Acids

c)

Amino Acids

d)

Nucleotides

17.
Amino acids all have the same general structure except for the:
a)
Amino Group
b)
Carboxyl Group
c)
'R' Group
d)
Carbonyl Group
18.

Cellulose, starch and glycogen are examples of:

a)

monosaccharides

b)

disaccharides

c)

lipids

d)

polysaccharides

19.

What is the following molecule?

a)

triglyceride

b)

phospholipid

c)

steroid

d)

protein

20.

What is the following molecule?

a)

alpha glcuose

b)

beta glucose

c)

amino acid

d)

disaccharide

21.

What is the following molecule?

a)

glucose

b)

DNA

c)

amino acid

d)

disaccharide

22.

Which protein structure describes the sequence of amino acids?

a)

Primary structure

b)

Secondary structure

c)

Tertiary structure

d)

Quaternary structure

23.

Which of the following describes the secondary structure of proteins?

a)

The sequence of amino acids

b)

The α-helix and β-pleated sheet folding

c)

The folding of the polypeptide chain due to the 'R' groups

d)

The joining of different protein molecules to make one big molecule

24.

Which protein structure describes a protein's three-dimensional shape?

a)

Primary structure

b)

Secondary structure

c)

Tertiary structure

d)

Quaternary structure

25.

Haemoglobin is a quaternary protein because:

a)

It has more than one peptide bonds

b)

Its shape is globular

c)

It consists of more than one polypeptide chains

d)

It has iron in each heme group