BIOLOGY NAME: ________________

Roll NO._______________
1st Year
REVISION AND LECTURE NOTES DATE: _________________

Chapter No.3 (STUDENT COPY)

Biology

MULTIPLE CHOICE QUESTION

1. If non-protein part is loosely attached to the protein part, it is known as:
(Lhr-2005: Guj-14GI, 15GII)

(A) Cofactor (B) Coenzyme (C) Holoenzyme (D) Prosthetic group

2. The vitamins are essential raw material for the synthesis of: (Swl-GI-2014)
(A) Activators (B) Co-factors (C) Co-enzymes (D) Prosthetic group
3. The detachable cofactors of an enzyme is known as: (Guj-GII-2014)
(A) Activator (B) Prosthetic group (C) Coenzyme (D) Apo enzyme
4. Enzymes involved in respiration, are found in: (Mtn-GI-2014)
(A) Chloroplasts (B) Ribosome (C) Mitochondria (D) Substrate
5. Metals ions are related to: (Guj-GI-2015)
(A) Coenzymes (B) Vitamins (C) Cofactors (D) Substrate
6. An activated enzyme with a co-enzyme is called: (Sgd-GI-2015)
(A) Holoenzymes (B) Coenzymes only (C) Apoenzymes (D) Activators
7. If the non-protein part of enzyme is covalently bonded, then it is called: (Sgd-GII-201: Rwp-GI-16)
(A) Co-factor (B) Activator (C) Co-enzyme (D) Prosthetic group
8. The inorganic and detachable cofactors are called: (Ajk-GI-2016)
(A) Activators (B) Coenzymes (C) Prosthetic groups (D) Inhibitors
9. Coenzymes are closely related to: (Mtn-GI-2016)
(A) Amino acids (B) Non protein particles (C) Vitamins (D) Enzymes
10. The non-protein part of enzyme is known as: (Guj-2007)
(A) Activator (B) Coenzyme (C) Cofactor (D) Polypeptides
11. Non-protein part attached to enzyme is called: (Mtn-2005)
(A) Coenzyme (B) Apoenzyme (C) Cofactor (D) Subtract
12. An enzyme with its coenzyme on prosthetic group removed is designated as: (Mtn-2004)
(A) Apoenzyme (B) Holoenzyme (C) Cofactor (D) Activator
13. An enzyme is a three dimensional protein: (Mtn-2005)
(A) Fibrous (B) Straight (C) Globule (D) Branched
14. Some enzymes use metal ions as cofactor like: (Mtn-2005)
(A) Mg2+ (B) Fe2+ (C) Cu2+ (D) All a, b, c

1
15. An activated enzyme consisting of polypeptide chain and a cofactor is known as:
(Fbd-2007: Guj-GII-16)
(A) Apoenzyme (B) Holoenzyme (C) Enzyme (D) Coenzyme
16. The activation energy of the reaction is lowered by: (Ajk-GI-2016)
(A) Co-enzyme (B) Enzyme (C) Substrate (D) Product
17. Enzyme lowers down the energy of: (Guj-GI-2016)
(A) Kinetic (B) Potential (C) Activation (D) Ionic
18. Lock and key model was proposed by: (Fbd-GI-2014: Rwp-GI-15)
(A) Koshland (B) Emil Fischer (C) Flemming (D) Watson
19. Three dimensional globular protein is: (Fbd-GI-2015)
(A) Starch (B) Glucose (C) Antibiotic (D) Enzyme
20. According to lock and key model, the active site is: (Lhr-GII-2015: Dgk-GII-16)
(A) Soft structure (B) Flexible Structure (C) Attractive Structure (D) Rigid Structure
21. Induced fit model was proposed by: (Lhr-GI-2015: Sgd-GI-16)
(A) Emil Fischer (B) Koshland (C) Jenner (D) Pasteur
22. Optimum pH for the proper functioning of enzyme sucrose is: (Bwp, Sgd-GI-2014)
(A) 2.00 (B) 4.50 (C) 5.50 (D) 7.60
23. The optimum pH of salivary amylase is: (Lhr-GI-2014: Dgk-GI-16)
(A) 2.80 (B) 4.80 (C) 6.80 (D) 8.80
24. The optimum pH of enzyme pepsin is: (Bwp-GI-2015: Lhr-GII-16)
(A) 2 (B) 6.8 (C) 7 (D) 9
25. The enzyme with optimum pH = 7.60 is: (Mtn-GI-2015)
(A) Arginase (B) Enterokinase (C) Catalase (D) Sucrase
26. The Optimum temperature of human body enzyme is: (Dgk-GI-15: Lhr-GI-14)
(A) 27Cº (B) 37Cº (C) 47Cº (D) 57Cº
27. A Little change in pH may lead to: (Dgk-GII-2015)
(A) Ionization of active sites of enzyme
(B) Ionization of substrate
(C) Retard or even block enzyme activity
(D) Effects enzyme only in high concentration
28. The optimum pH of Exterokinase is: (Swl-GI-2016)
(A) 1.50 (B) 3.50 (C) 5.50 (D) 7.50
29. Optimum pH of value for enzyme pepsin is: (BWP-G1)-16
(A) 4.50 (B) 9.00 (C) 2.00 (D) 5.50
30. Which is the example of competitive inhibitor? (Fbd-2007)
(A) Fumaric acid (B) Succinic acid (C) Malonic acid (D) None of these
31. The active site of an enzyme: (Mtn-2008)
(A) Never change
(B) Form no chemical bond with substrate
(C) Determine by its structure the specificity of enzyme
(D) Looks like a lump projecting from surface of an enzyme
32. If more substrate to an already occurring enzymatic reaction is added, more enzyme
activity is seen because
(A) Then is probably more substrate present than there is enzyme.

2
 (B) Then is probably more enzyme available than there is substrate.
(C) Then is probably more product present than their in either substrate or enzyme.
(D) The enzyme substrate complex is probably failing to form during the reaction.
33. What if you add more substrate to already occurring enzymatic reaction and it has
no effect on the rate of reaction? What is the form given for this situation?
(A) Saturation (B) Denaturation (C) Composition (D) Inhibition
34. The rate of an enzyme-catalyzed reaction:
(A) Is constant under all conditions (B) Decrease as substrate concentration increase
(C) Cannot be measured (D) Can be reduced by inhibitors
35. The active site of an enzyme:
(A) Never changes
(B) Forms no chemical bond with substrate
(C) Determines, by its structure, the specificity of the enzyme
(D) Looks like a lump projecting from the surface of an enzyme
36. Which statement about enzyme is not true?
(A) They consist of proteins, with or without a non-protein part.
(B) They change the rate of catalyzed reaction.
(C) They are sensitive to heat.
(D) They non-specific in their action.
37. Enzymes involved in cellular respiration are found in:
(A) Cytoplasm (B) Mitochondria (C) Nucleus (D) Ribosome
38. The inactive form of enzyme pepsin is:
(A) Holoenzyme (B) Simple enzyme (C) Pepsinogen (D) None
39. Template model of enzyme action is:
(A) Lock & key model (B) Induce fit model (C) Scale Model (D) None
40. Which one of the following is an enzyme inhibitor?
(A) Cyanide (B) Antibiotics (C) Anti-metabolites (D) All

Scientists

Sr. No. Year Scientists Contributions Page No.

1 1890 Emil Fischer Lock and key model of enzyme
action
2 1959 Daniel Koshland Induce fit model

3
 QuestionS
1. Define Enzyme
Ans.
The proteinaceous substances which speed up biochemical reactions without being used
up arc known as enzymes. e.g. trypsin, pepsin, amylase, etc.
2. Define co-factor.
Ans.
Enzymes are made up of proteins but some enzymes consist of non-protein part too. The
non-protein part of an enzyme is known as co-factor.
 It helps in proper functioning of enzymes.
 It usually acts as a bridge between the enzyme and substrate.
 It may also acts as a source of chemical energy for the reaction.
 It is of three types:
 Activator
 Co-enzyme
 Prosthetic group
3. Define aponzyme and holoenzyme.
Ans.
Apoenzyme (Greek apo meaning "incomplete")
An enzyme with its co-enzyme or prosthetic group removed is known as apoenzyme. In
other words, the protein part of an enzyme is known as apoenzyme. It is inactive form of
an enzyme.
Holoenzyme (Greek bolo meaning "complete")
An activated enzyme consisting of a protein part and a co-factor is known as
holoenzyme. It is active form of an enzyme.
4. How an enzyme accelerates a biochemical reaction?
Ans.
Enzymes are metabolically active proteins which speed up biochemical reactions, without
being used up. They accelerate a biochemical reaction by lowering its activation energy.
5. Write four characteristics of enzymes.
Ans.
 Enzymes are composed of globular proteins.
 They speed up biochemical sections-without being used up.
 They are very specific in their actions. i.e they are substrate specific.
 Some enzymes need non-protein part co-factor for proper functioning.
 Enzymes work by lowering activation energy of reaction.
 They need aqueous medium for their activity.
6. Define active site of an enzyme.
Ans.

4
 The portion of an enzyme which has catalytic activity and to which substrate attaches is
called active site.
It is a three-dimensional cavity and is often charged. It is formed by specific amino acids.
Active site comprises of two regions:
Binding site
Catalytic site
7. What do you know about binding site and catalytic site?
Ans.
Building Site
It is the portion of active site that helps in the recognition or identification of substrate. It
also helps in the binding of substrate Hence ES complex is formed.
Catalytic Site
It is the portion of active site which catalyzes the transformation of the substrate into
products. The enzyme after catalysis detaches itself unchanged.
8. What is meant by the optimum pH of an enzyme?
Ans.
The narrow range of pH at which an enzyme works at its maximum rate is called
optimum pH.
Examples
 Optimum pH for pepsin is 2.00
 Optimum pH for sucrose is 4.5
 Optimum pH for arginase is 9.7
9. Define inhibitor. Give examples.
Ans.
A chemical substance that inhibits the enzyme activity either by blocking active site or by
destroying its globular structure is called an inhibitor.
The inhibitor may block the active site temporarily or permanently.
e.g. cyanide, antibiotics, antimetabolites, drugs, mercury etc.
10. Why competitive inhibitors fail to from the products?
Competitive inhibitors fail to from the products because they may be selected by building
site due to their structure similarity with substrate but are not able to activate the catalytic
site. They are not the actual substrates. That is why products are not formed.

IMPORTANT SHORT QUESTION

Apoenzyme Holoenzyme
Without co-factor With cofactor
Inactive Active
Enzyme Optimum pH
Pepsin 2.00
Sucrose 4.50
Enterokinase 5.50
Salivary amylase 6.80

5
Catalase 7.60
Chymotrypsin 7.00-8.00
Pancreatic lipase 9.00
Arginase 9.70
Competitive inhibitors Non-competitive inhibitors
Attack on active site Attack on other site
Structurally similar with substrate Structurally dissimilar with substrate
e.g., Malonic acid etc. e.g., Cyanide
Enzyme Co-enzyme
The proteinaceous substance which speed up It is non-protein part of enzyme that is organic in
biochemical reactions without being used up are nature.
called enzyme.
It is either composed of only protein or a It is loosely attached to the protein part of
combination of protein and non-protein part. enzyme.
e.g., trypsin, pepsin etc. Co-enzymes are derived from vitamins.
e.g., NAD
Lock and Key Model Induced Fit Model
It was proposed by the Emil Fisher in 1890 It was presented by Koshland in 1959.
According to this model, a specific key can open According to this model, when a substrate
only a specific lock, similarly a specific enzyme can combines with an enzyme, it induces change in the
transform a specific substrate into the product enzyme structure. This change enables the enzyme
to perform catalysis effectively.
Active site is a rigid structure and it is used only as Active site is not rigid.
a template.
Latest studies did not support it. It is based on latest research.
Reversible inhibitors Irreversible inhibitors
They bind to enzymes by weak linkages. They bind to enzymes permanently by covalent
bond.
They temporarily attach to enzyme. They either block active site or destroy globular
structure permanently.
e.g., Malonic acid, Cyanide etc. e.g., Hg etc.

IMPORTANT LONG QUESTION

1. Describe the characteristics of enzymes in detail.
2. Describe mechanism of enzyme action in detail.
3. What are inhibitors? Explain its types.