LECT – 16- 21 Enzymes - Properties, classification and nomenclature

I. Choose the best answers

1. The followings enzymes is not protein

a. Diastase b. Pepsin c. Ribozymes d. Trypsin

2. Lock and Key model was proposed by

a. Pasteur b. Fischer c. Koshland d. Kuhne

3. Induced fit model was proposed by

a. Sanger b. Fischer c. Koshland d. Kuhne

4. The metal ions which are loosely attached with the enzymes are called:

a. Coenzyme b. Prosthetic groups c. Cofactors d. Apoenzyme

5. The non protein, organic molecules that participate in enzyme-catalyzed reactions is:

a. Holoenzyme b. Prosthetic groups c. Cofactors d. Coenzyme

6. The covalently bonded non-protein part cofactors are called

a. Coenzyme b. Prosthetic groups c. Cofactor’s d. None

7. NAD is:

a. Coenzyme b. Prosthetic groups c. Cofactors d. None

8. Which of the followings is hydrolyze enzyme?

a. Ribozyme b. Diastase c. Hydrase d. Mutase

9. Epimers are:

a. Ribozyme b. Diastase c. Hydrolase d. Isomerase

10. The enzyme which joins

a. Isomerase b. Ligase c. Transferase d. Mutase

11. Which of the following is the correct Line weaver-Burk equation?

Answer: A
12. When the velocity of enzyme activity is plotted against substrate concentration, which of the
following is obtained?

a. Parabola

b. Hyperbolic curve (At low substrate concentration, the rate of a reaction is determined by the
rate of formation of an enzyme-substrate complex)

c. Straight line with positive slope

d. Straight line with negative slope

13. Which of the following is true about Michaelis-Menten kinetics?

a. Km, the Michaelis constant, is defined as that concentration of substrate at which enzyme is
working at maximum velocity

b. Km, the Michaelis constant is defined as the dissociation constant of the enzyme-substrate
complex

c. It describes single substrate enzymes (Km is defined as that concentration of substrate at

which enzyme is working at half of maximum velocity. It is also a measure of the affinity that
the enzyme has for its substrate. Michaelis-Menten kinetics assumes non-covalent binding
between enzyme and substrate).

d. It assumes covalent binding occurs between enzyme and substrate

14. Which of the following statements is true about competitive inhibitors?

a. It is a common type of irreversible inhibition

b. In the presence of a competitive inhibitor, the Michaelis-Menten equation becomes

(Competitive inhibition is a common type of reversible inhibition. The apparent

Km increases in the presence of inhibitor by a factor α. The maximum velocity for the reaction
remains same in the presence of a competitive inhibitor).

c. The apparent Km decreases in the presence of inhibitor by a factor α

d. The maximum velocity for the reaction decreases in the presence of a competitive inhibitor

15. Which of the following statements is true about uncompetitive inhibitors?

a. They bind covalently at a site distinct from the substrate active site

b. Apparent Km also increases

c. They increase the measured Vmax⁡

d. In the presence of a uncompetitive inhibitor, the Michaelis-Menten equation becomes

(They bind non-covalently at a site distinct from the substrate active site. They decrease the
measured Vmax⁡ and also apparent Km).

16. The rate determining step of Michaelis-Menten kinetics is

a. The complex dissociation step to produce products (The breakdown of ES complex is the
rate determining step of Michaelis Menten kinetics).

b. The complex formation step

c. The product formation step

d. None of the above

17. The molecule which acts directly on an enzyme to lower its catalytic rate is

a. Repressor b. Inhibitor c. Modulator d. Regulator

(An inhibitor is a substance which interferes with the substrate-active site binding and slows
down the catalytic rate).

18. Which of the following is an example for irreversible inhibitor?

a. Disulfiram b. Oseltamivir c. Protease inhibitors d. DIPF

(Disulfiram, Oseltamivir and protease inhibitors are reversible inhibitors).

19. Which of the following is an example of reversible inhibitor?

a. DIPF b. Penicillin c. Iodoacetamide d. Protease inhibitors

(DIPF, Penicillin and Iodoacetamide are irreversible inhibitors).

20. Where does inhibitor binds on enzyme in mixed inhibition?

a. At active site

b. Allosteric site

c. Does not bind on enzyme

d. Binds on substrate

21. The catalytic efficiency of two distinct enzymes can be compared based on which of the
following factor?

a. Km

b. Product formation
c. Size of the enzymes

d. pH of optimum value

22. What is the general mechanism of an enzyme?

a. It acts by increasing the activation energy

b. It acts by reducing the activation energy

c. It acts by decreasing the pH

d. It acts by increasing the pH

23. The polypeptide chains in chymotrypsin are linked by

a. Hydrogen bonds

b. Ionic bonds

c) Disulfide bond

d. SH-SH bond

24. Which of the following catalyzes the reversible degradation of 2-phosphoglycerate to

phosphoenol pyruvate?

a. Chymotrypsin b. Hexokinase c. Enolase d. Trypsin

25. Which of the following catalyzes the reversible reaction of β-D-Glucose to glucose 6-
phosphate?

a. Chymotrypsin b. Hexokinase c. Carboxylase d. Renin

26. The allosteric inhibitor of an enzyme

a. Causes the enzyme to work faster
b. Binds to the active site
c. Participates in feedback regulation
d. Denatures the enzyme

(In feedback regulation, enzyme is not directly inhibited by the end product instead its synthesis
is inhibited by interfering with the gene of that enzyme).

27. Removal of phosphoryl groups is catalyzed by

a. Diphteria toxin and cholera toxin

b. Dinitrogenase reductase

c. Protein kinases
d. Protein phosphatases

(The enzymes that catalyze the ADP-ribosylation and inactivation of key cellular enzymes or
proteins are diphteria toxin and cholera toxin.

Dinitrogenase reductase is responsible for the regulation of biological nitrogen fixation.

The attachment of phosphoryl groups to specific amino acid residues is catalyzed by protein
kinases).

28. Which of the following takes place due to phosphorylation of isocitrate dehydrogenase?

a. Inhibits the binding of citrate at active site

b. Degrades the enzyme

c. Enhances the substrate-binding affinity

d. No reaction

29. How many types of enzymatic regulation mechanism occurs in the cells?

a. 2 b. 3 c. 4 d. 5

(Feedback inhibition, reversible covalent modification of enzymes, proteolytic activation of

enzyme, feedback regulation and regulation of isozymes).

30. Bile salts and a cofactor is called as

a. Lipase b. Pancreatic Lipase c. Colipase d. Phospholipase

31. _______ are calcium dependent hydrolyase class of metaloenzyme that catalyzes the
hydrolysis of 1, 4- α-glycosidic linkages in polysaccharides.

a. α-Amylase b. Calmodulin c. β-Amylase d. Phosphorylase

32. Isozymes arise through ................ duplication

a. gene b. mutants c. clonal d. none of the above

33. Examples of Isoenzymes

a. MDH b. GDH c. LDH d. PDH

34. Physically distinct forms of the same enzyme are called as

a. Abzymes b. Synzymes c. Coenzymes d. Isoenzymes

35. The optimum pH of alkaline phosphatase are

a. 9-10 b. 7-8 c. 4-5 d. 6-7

36. What is the unit of Vmax?

a. mmol/s b. µmol/s c. mol/s d. g/mol

37. Where are enzymes located?

a. Cytoplasm b. Golgi complex c. ER d. Ribosomes

38. Some herbicides are used to block plant enzyme activity. A tiny herbicide molecule can
attach to the _______of an enzyme and stop it from working.

a. Allosteric site b. Catalytic site c. Active site d. Substrate

39. Which enzymes reduce polysaccharides to disaccharides: lactose, maltose, and sucrose

a. Lactase b. Amylase c. Sucrase d. Maltase

40. The enzymes which digest specific carbohydrate bonds found in fiber

a. Hemicellulase b. Amylase c. Cellulase d. Dextrins

41. Break down of long protein chains into smaller amino acid chains and eventually into single
amino acids

a. Peptidase b. Aminoprotease c. Protease d. Alkaline protease

42. The International Union of Biochemistry (I.U.B.) initiated standards of enzyme nomenclature
which recommend that enzyme names indicate both the substrate acted upon and the type of
reaction catalyzed names end as

a. ase b. ose c. in d. ol

43. The enzyme will act on a particular type of chemical bond regardless of the rest of the
molecular structure.

a. Absolute specificity

b. Group specificity

c. Linkage specificity

d. Stereochemical specificity

44. The rate is independent of substrate concentration is

a. Zero order b. First order c. Second order d. No order substrate reactions

45. The rate = k[S] [S] =k[S]2 of reaction is proportional to the square of the substrate
concentration

a. Zero order b. First order c. Second order d. None of the above

46. Transfer of amine group from one molecule to another is

a. Transferase b. Transaminase c. Transketolase d. Transacetylase

47. _______ is natural nutrient for the soil. Vegetable can grow healthily within a short period.

__________ are organic substances produced by beneficial microbes.

a. Enzymes b. Substrate c. Amylase d. Cellulase

48. Fruits contain enzymes. Fruits like papaya, kiwifruit, pineapple and figs all contain enzymes
called

a. Galactouranase b. Protease c. Amylase d. Cellulase

49.

50. Which enzymes present in apple

a. polyphenol oxidase b. Amylase c. cellulose d. gluco amylase

==================================================================

Enzyme names always end in -ase

Lipase = for fat

Lactase = for milk sugars

Peptidase, Protease = for protein

Amylase = Starches
=================================================================

Fill in blanks

1. Most enzymes are proteins. Some are nucleic acids (RNA) like _____ (Ribozyme)

2. ________ proposed the lock and key model in 1890. (Emil Fischer)

3. The metal ions which are loosely attached with the enzymes are called
_________(Cofactors)

4. _________ are non protein, organic molecules that participate in enzyme-catalyzed

reactions. (Coenzymes)

5. The covalently bonded non-protein part cofactors are called________ group. (Prosthetic)
6. __________ enzymes change their structure in response to binding of effectors.
(Allosteric)

7. The inactive enzyme without prosthetic group is called _____ (Apoenzyme)

8. The active enzyme with attached prosthetic group is called_____ (Holoenzyme)

9. ________are proteins with different structure which catalyze the same reactions
(Isozymes or Isoenzymes)

10. The SI unit of katal is kg-1 but µmol mg-1 min-1 is commonly used.

11. Enzyme activity is moles of substrate converted per unit time. The SI unit is ____ (Katal)

12. 1 katal is equal to how much ________ (1 mol s-1)

13. _________ serves as cofactor for carbonic anhydrase and alcoholdehydrogenase (Zn2+)

14. The cofactor for ferredoxin, hemoglobin and cytochrome is known as ______ (Fe+/Fe3+)

15. The enzyme catalyzes only one reaction _______________ (Absolute Specificity)

16. The maximum number of substrate molecules converted to product per enzyme molecule
per second __________ (Turnover number)

17. The __________ plot or double reciprocal plot is a linear form of the Michaelis–Menten
equation (Lineweaver – Burk)

18. Ions tightly bound are known as __________ (Metalloenzymes)

19. ___________ equation describes the relationship between the reaction rate and substrate
concentration (Michaelis Menten)

20. __________are certain molecules that can decrease the catalytic rate of an enzyme-
catalyzed reaction (Inhibitors)

21. _______ refer to loosely bound coenzymes that are released in the same way as substrates
and products (Cosubstrates)

22. The enzyme structure are altered for subsequent reactions Cosubstrates)

23. Enzymes with ping–pong mechanisms include some oxidoreductases such as ____
(thioredoxin peroxidase)

24. ________are molecules that reduce or abolish enzyme activity (Enzyme inhibitors)

25. determined as Rate constants

Name the following:

1. The biological catalysts which accelerate the rate of biochemical reactions-

ENZYMES.
2. The chain of reactions in enzymes - METABOLIC PATHWAY.
3. The enzyme containing amino acids only -APOENZYME.
4. A non-protein group-PROSTHETIC GROUP.
5. The enzyme molecule consisting of protein and prosthetic group-HOLOENZYME.
6. The prosthetic group which is inorganic -COFACTOR.
7. The prosthetic group which is organic -COENZYME.
8. The metals known to be cofactors of enzyme- COPPER, IRON, MAGNESIUM,
ZINC, CALCIUM, POTASSIUM AND COBALT.
9. A coenzyme- NAD, FAD, NADP, CoA, FMN.
10. They can catalyze wide range of reactions- INORGANIC CATALYST.
11. They catalyze specific reaction of substrates-ENZYMES.
12. The term enzyme was coined by- KUHNE.
13. Enzyme present in papaya- PAPAIN.
14. Short names given to enzymes-RECOMMENDED NAMES.
15. They can oxidize their substrate by addition of oxygen and removal of hydrogen-
OXIDOREDUCTASES OR DEHYDROGENASE.
16. These enzymes bring about transfer of functional group- TRANSFERASES.
17. These enzymes catalyze the hydrolysis of their substrate by adding water-
HYDROLASE.
18. These enzymes catalyze the removal of groups from their substrate- LYASES.
19. These enzymes catalyze the linking together of compounds- LIGASES OR
SYNTHETASES, POLYMERASE.
20. The substance on which an enzyme acts-SUBSTRATE.
21. The substance obtained in the end of chemical reaction- PRODUCT AND
ENZYME.
22. The minimum energy required to start a chemical reaction- ACTIVATION
ENERGY.
23. The 3D structure of the protein imparts shape to the enzyme- ACTIVE SITE.
24. The site of an enzyme where the substrate joins to-active site.
25. What are the three ways by which the enzyme becomes inactive- competitive, non-
competitive, negative feedback mechanism or allosteric inhibitors.
26. By what substance does the enzyme become inactive- Inhibitors.
27. Who is the founder of the lock and key theory- EMIL FISCHER.
28. Enzymes react with substrate to form- INTERMEDIATE COMPLEX OR
ENZYME SUBSTRATE.
29. Proteins that contains amino acids only – simple protein molecule
30. Name the two types of conjugated molecules- apoenzyme and prosthetic group
31. What is the structure of the specific protein molecule called- 3 dimensional
structure.
32. Who founded the induced fit hypothesis- Dan koshland.
33. The breaking of molecules without the presence of water-lyase.
34. Splitting of organic matter with the help of water-hydrolase.
35. Changing the speed of reaction in a living organism-biocatalyst.
 36. Minimum energy required to start a chemical reaction –activation energy.
37. Where does the inhibitor fix itself during non-competitive enzyme inhibitors-
inhibitor site.
38. The study of the chemical reactions that are catalysed by enzymes – Enzyme
kinetics
39. The maximum rate of an enzyme catalysed reaction i.e. when the enzyme is saturated
by the substrate – Vmax
40. It is measure of how easily the enzyme can be saturated by the substrate - Km
41. It is a graphical representation of enzyme kinetics in which reaction rate is plotted as
a function of the ratio between rate and substrate concentration - Eadie-Hofstee Plot
42. It is a graphical representation of enzyme kinetics in which the ratio of the initial
substrate concentration [S] to the reaction velocity v is plotted against [S] - Hanes–
Woolf plot
43. A molecule is one that interacts with the enyzme, but usually not at its active site -
noncompetitive inhibitor
44. Any compound which closely resembles the substrate in its chemical structure and
molecular geometry - Competitive inhibitor
45. When an enzyme inhibitor binds only to the enzyme-substrate complex and thereby
ceases the enzyme from reacting with substrate to form product - Uncompetitive
inhibitor
46. The inhibitors usually covalently bind to the reactive functional groups of an
enzyme, which influence the catalytic activity of the enzyme- IRREVERSIBLE
INHIBITORS
47. Ribonucleic acid enzyme is an RNA molecule capable of catalyzing a chemical
reaction – Ribozyme
48. The term ribozyme was first introduced by Kelly Kruger et al. in 1982.
49. In 1902 Victor Henri proposed a quantitative theory of enzyme kinetics
50. German biochemist Leonor Michaelis and Canadian physician Maud Menten, who
investigated the kinetics of an enzymatic reaction mechanism, invertase, that
catalyzes the hydrolysis of sucrose into glucose and fructose.
====================================================================

Match the Following

Oxidoreductase a. Triose phosphate -4

Transferase b. Aldolase -5
Hydrolase c. Deaminase - 2
Isomerase d. Synthase - 6
Lyase e. Dehydrogenase - 1
Ligase f. Lipase - 3

Vo a. total enzyme concentration - 3

ES b. initial velocity -1
ET c. Michaelis constant - 4
Km d. concentration of enzyme substrate
complex - 2
Proteases a. a polysaccharide found in plant cell
walls - 4
Amylases b. break triglycerides into individual fatty
acids and glycerol -3
Lipases c. reduce polysaccharides to
disaccharides -2
Pectinase d. break long protein chains into smaller
amino acid chains and eventually into
single amino acids -1

Alpha-galactosidase a. Starches -2
Amylase b. Maltose, the sugar in grains - 4
Cellulase c. Carbohydrates in legumes that cause
flatulence -1
Glucoamylase d. Cellulose (fiber) in fruits, vegetables,
grains, and seeds -3

Name the Site of Enzymes – Substrate complex

Active Site 1. Enzyme where substrate molecules bind

and undergo a chemical reaction - C
Catalytic site 2. area of an enzyme where the substrate
binds and the chemical reaction takes
place - A
Binding Site 3. regulation of an enzyme by binding an
effector molecule - D
Allosteric Site 4. Enzyme residues that catalyse a reaction
of that substrate - B
Cofactors a. TPP - 2
Coenzymes b. Catalytic RNA molecules - 4
Isozymes c. Biotin - 1
Ribzymes d. LDH - 3

papain a. Corn -3
bromelain b. Legumes - 4
xylanase c. Pineapple -2
alpha-galactosidase d. raw papaya -1

=====================================================================

Amylase – breaks down carbohydrates, starches, and sugars which are prevalent in potatoes,
fruits, vegetables, and many snack foods

• Lactase – breaks down lactose (milk sugars)

• diastase – digests vegetable starch
• sucrase – digests complex sugars and starches
• maltase – digests disaccharides to monosaccharides (malt sugars)
• invertase – breaks down sucrose (table sugar)
• glucoamylase – breaks down starch to glucose
• alpha-galactosidase – facilitates digestion of beans, legumes, seeds, roots, soy products, and
underground stems

Protease – breaks down proteins found in meats, nuts, eggs, and cheese

• pepsin – breaks down proteins into peptides

• peptidase – breaks down small peptide proteins to amino acids
• trypsin – derived from animal pancreas, breaks down proteins
• alpha – chymotrypsin, an animal-derived enzyme, breaks down proteins
• bromelain – derived from pineapple, breaks down a broad spectrum of proteins, has anti-
inflammatory properties, effective over very wide pH range
• papain – derived from raw papaya, broad range of substrates and pH, works well breaking
down small and large proteins

• Lipase – breaks down fats found in most dairy products, nuts, oils, and meat

• cellulase – breaks down cellulose, plant fiber; not found in humans

Other stuff

• betaine HCL – increases the hydrochloric acid content of the upper digestive system; activates
the protein digesting enzyme pepsin in the stomach (does not influence plant- or fungal-derived
enzymes)
• CereCalase™ – a unique cellulase complex from National Enzyme Company that maximizes
fiber and cereal digestion and absorption of essential minerals; an exclusive blend of synergistic
phytase, hemicellulase, and beta-glucanase
• endoprotease – cleaves peptide bonds from the interior of peptide chains
• exoprotease – cleaves off amino acids from the ends of peptide chains
• extract of ox bile – an animal-derived enzyme, stimulates the intestine to move
• fructooligosaccharides (FOS) – helps support the growth of friendly intestinal microbes, also
inhibits the growth of harmful species
• L-glutamic acid – activates the protein digesting enzyme pepsin in the stomach
• lysozyme – an animal-derived enzyme, and a component of every lung cell; lysozyme is very
important in the control of infections, attacks invading bacterial and viruses
• papayotin – from papaya
• pancreatin – an animal-derived enzyme, breaks down protein and fats
• pancrelipase – an animal-derived enzyme, breaks down protein, fats, and carbohydrates
• pectinase – breaks down the pectin in fruit
• phytase – digests phytic acid, allows minerals such as calcium, zinc,
copper, manganese, etc. to be more available by the body, but does not break down any food
proteins
• xylanase – breaks down xylan sugars, works well with grains such as corn

=================================================================

Descriptive Questions

1. Define enzymes.
An enzyme is a biological catalyst that can accelerate a specific chemical reaction by lowering
the activation energy but remain unaltered in the process.

2. What is the chemical nature of enzyme?

Most enzymes are proteins. Some are nucleic acids (RNA) like

3. What is active site of enzyme? Give its function.

An active site is the part of an enzyme that directly binds to a substrate and carries a reaction.

In the active site, amino acids of the enzyme protein will bind to the substrate.

4. What are the components of active site?

The active site has two components:
Binding site: It recognizes the specific substrate and forms enzyme substrate complex. This
reaction activates the catalytic site.
Catalytic site: The activated catalytic site changes the substrate into products.

6. What is lock and key model?

Emil Fischer proposed the lock and key model in 1890. According to this model a specific
enzyme can transform only specific substrate into products. According to this model, the active
site is a rigid structure. It cannot be changed during any step of the reaction.

7. What is induced fit Model? Give its significance.

This model was proposed by Koshland in 1959. He proposed this model on the basis of new
evidences, lie describes that when a substrate combines with an enzyme, it induces changes in
the active site.
8. What are cofactors? Give examples.
The metal ions which are loosely attached with the enzymes are called cofactors. These metal
ions are Ca++, Mg++. Mn+, Cu+, and Zn–.

9. Differentiate between coenzyme anti prosthetic groups.

Coenzymes are non protein, organic molecules that participate in enzyme-catalyzed reactions.
The covalent bonded non-protein part cofactors are called prosthetic group.

10. What is allosteric site? Give its function.

Some enzymes have special allosteric site. Some specific effectors can bind with this allosteric
site. Allosteric enzymes change their structure in response to binding of effectors.

11. Differentiate between apoenzyme and holoenzyme.

Some enzymes require prosthetic group for their normal activities. Prosthetic group is firmly
bound to the enzyme. An apoenzyme is an inactive enzyme, activation of the enzyme occurs
upon binding of an organic or inorganic cofactor. Holoenzyme - An apoenzyme together with its
cofactor. A holoenzyme is complete and catalytically active. Most cofactors are not covalently
bound but instead are tightly bound.

12. What are Oxidoreductases? Give examples.

An oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the
reductant, also called the electron donor, to another, the oxidant, also called the electron
acceptor. This group of enzymes usually utilizes NADP or NAD+ as cofactors. They are further
subdivided into oxidases, peroxidases, catalases, dehydrogenases and reductase.

13. What are Hydrolases? Give two examples.

These enzymes catalyses the hydrolysis of the molecules of organic foods, polysaccharides, fats
and proteins. In the process the large food molecules are split into smaller fragments by the
addition of water. Thus these enzymes are also called digestive or hydrolytic enzymes.
Examples: Maltase, pepsin.
14. What is activation energy? How is it lowered?

Activation energy is the minimum energy that is required to start a reaction. Enzyme lowers the
activation of energy. The reaction can take place in the absence of enzyme. But it needs higher
amount of activation energy.

15. What are ligases? Give their function?

These enzymes link two molecules along with the breakdown of a pyrophosphate bond (PP) of
ATP. They are also called synthetases.

16. What are Lyases enzymes?

A lyase is an enzyme that catalyzes the breaking (an "elimination" reaction) of various chemical
bonds by means other than hydrolysis (a "substitution" reaction) and oxidation, often forming a
new double bond or a new ring structure. The reverse reaction is also possible (called a "Michael
addition").

17. What are the different classes of enzymes?

Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases, and Ligases. This is the

international classification used for enzymes. Enzymes are normally used for catalyzing the
transfer of functional groups, electrons, or atoms.

18. What are the three different types of enzymes?

Proteases and peptidases split proteins into small peptides and amino acids.
Lipases split fat into three fatty acids and a glycerol molecule.
Amylases split carbohydrates such as starch and sugars into simple sugars such as glucose.
Nucleases split nucleic acids into nucleotides.
19. What are the main categories of enzymes?
Enzymes appear in the subcategory Category: Enzymes by function according to the EC number
classification:
EC 1 Oxidoreductases: catalyze oxidation/reduction reactions
EC 2 Transferases: transfer a functional group (e.g. a methyl or phosphate group)
EC 3 Hydrolases: catalyze the hydrolysis of various bonds
EC 4 Lyases: cleave various bonds by means other than hydrolysis and oxidation
EC 5 Isomerases: catalyze isomerization changes within a single molecule
EC 6 Ligases: join two molecules with covalent bonds
20. Define Turnover Number
The number of substrate molecules on which one enzyme molecule acts in one second is called
Turnover over number.

21. What is Substrates?

An enzyme is extremely selective for the reaction. The reactants of enzymatic reactions are
called substrates.

22. Why is this enzyme important to plants?

Green plants make their own organic molecules however other organisms need to obtain their
food readymade. Extracellular digestion occurs when an organism secretes enzymes to digest the
surrounding material. It releases amylase enzymes to digest the starch into maltose and then
absorbs the maltose.

23. What does the Michaelis Menten equation tell us?

Km is the Michaelis-Menten constant which shows the concentration of the substrate when the
reaction velocity is equal to one half of the maximal velocity for the reaction. It can also be
thought of as a measure of how well a substrate complex with a given enzyme, otherwise known
as its binding affinity.

24. What does the Michaelis Menten model determined?

The Michaelis-Menten model (1) is the one of the simplest and best-known approaches to
enzyme kinetics. KM (the Michaelis constant; sometimes represented as K S instead) is the
substrate concentration at which the reaction velocity is 50% of the Vmax[S] is the concentration
of the substrate S.

25. What is km in enzyme kinetics?

Km and Vmax are related to enzyme kinetics in a biological system. K m is the substrate
concentration that is required for the reaction to occur at 1/2 V max. In other words, it is how much
substrate is needed for the reaction to occur at 1/2 its max possible rate.
Difference between Enzymes, nomenclature, inhibition and applications
Apoenzyme
1. Composed of proteins (amino acids)
only.
2. The present protein is called amino acids
Coenzyme
1. Necessary for the functioning of an
enzyme
2. Its an organic compound
3. Eg:- NAD,FAD,FMN,coA
Enzyme
1. They are specific protein molecules
with complex 3D structures.
2. They can catalyse only specific
reaction of single or structurally
related substrates.
3. Their catalytic action can be
regulated by specific regulating
molecules
4. They are very sensitive to change in
PH and temp.
Hydrolase
1. Break the substrate using water
2. Substrate may be esters, peptides
and etc.
3. Reaction leaves a single bond
Prosthetic group
1. A non-protein group
2. The enzyme molecule consists of
proteins and the prosthetic group is called
holoenzyme.
Cofactor
1. Associated with the catalytic
properties for the enzyme.
2. Its an inorganic compound
3. Eg:- metals, glycolysis
Inorganic catalyst
1. Hey are small inorganic molecules
2. They can catalyse wide range
reactions.
3. Their catalytic action cannot be
regulated by any regulating
molecule.
4. They are less sensitive to PH and
temperature changes.
Lyases
1. Break the substrate without using
water.
2. Substrate may be histidine
decarboxylase breaks the covalent
bonds between carbon atoms.
3. Reaction leaves a double bond
Isomerase
1. The substrate is converted into
positional isomer by intercellular
changes.
2. Eg: - phosphohexoisomerase
catalyzes the conversion of glucose
6-phosphate into fructose 6-
phosphate.
Substrate
1. The substance on which the enzyme
acts is called substrate.
2. Substrates are particular to their
specific enzymes.
Lock and key
1. It said that substrate fits into the
active site of an enzyme like a key.
2. Enzymes are substrate specific and
only that particular substrate can fit
into that enzyme.
3. The theory didn’t explain the
flexibility of the active site.
4. Discovered by emil fitcher
Active site
1. Where a particular substrate fits into
for the reaction to proceed with the
products being formed and the
enzyme not getting altered.
Transferase
1. Brings transfer of functional group
other than hydrogen from one
group to another.
2. Eg: - glutamate pyruvate
transaminase catalyzes the shifting
of an amino group from glutamate
to pyruvate.
Enzyme inhibitors
1. Functional group capable of
interacting with other group
compounds.
2. They are not particular to specific
enzymes.
Induced fit
1. The active site of the enzyme is not
in the shape of the substrate but
does change when a specific
substrate comes to fit in.
2. The enzyme regains its original
shape before the reaction and then
starts the same process again.
3. The theory explained the flexibility
of the active site.
4. Discovered by Dan koshland
Allosteric
1. Any part on the enzyme where an
inhibitor has joined itself to the
enzyme reducing the flexibility of
the enzyme for a particular
substrate to fit in the active site and
inhibiting the further reaction.
Competitive
1. They are structural analogs that are
of the same structure of the
substrate to fit into the active site
before the substrate.
2. Takes the shape of the substrate
3. Instead of the formation of ES
complex EI complex is formed.
Enzyme
1. Biological catalyst altering the rate
of biochemical reactions in the body
2. To speed up or lower the reactions
3.
Activation energy
1. The minimum kinetic energy
required to stat up a chemical
reaction is called as the activation
energy.
Lyase
1. Removal of groups from their
substrate without using water.
2. Leaving double bond.
Non-competitive
1. They do not possess any structural
similarity with the substrate and do
not attach to the active site of the
enzyme.
2. Does not take the substrate shape
3. Restricts the flexibility of the active
site due to which the substrate is
unable to fit into the enzyme.
Hormone
1. They are chemicals released by the
respective glands.
2. To pass a message to the respective
gland to release their specific
hormone.
Turnover number
1. The number of moles of substrate
converted per minute by one mole
of enzyme is called turnover
number of an enzyme.
Ligase
1. Catalyse the linking together of
compounds utilizing the energy
ATP.
2. Leaving single bond.
Some common enzymes and their E.C. number :
Define the following:

1) Enzyme

2) Activation energy

3) Catalysis

4) Apoenzyme

5) Prosthetic group

6) Coenzyme

7) Isoenzyme

8) Competitive inhibition

9) Non-competitive inhibition

10) Allosteric inhibition

11) Feed-back inhibition

12) Holoenzyme

13) Lock and key hypothesis

14) Induced fit hypothesis

15) Michaelis constant

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Explain briefly:

1) Structure of enzyme

2) Mechanism of enzyme action

3) Basis of Enzyme nomenclature

4) Classification of enzyme

5) Properties of enzyme

6) Factors affecting enzyme activity

7) Inhibition of Enzyme action

8) Differences between competitive and Non-competitive inhibition

9) How does enzyme lower the activation energy?

10) Isoenzymes
11) Michaelis Menten Equation

12) Lineweaver Burk plot and Eadie–Hofstee Plot difference

13) What is the effect of PH on enzyme activity?

14) Types of Enzymes

i. Exo-enzymes: Enzymes that function outside the cell are called so, e.g. zymase, lysozyme,
digestive enzymes.

ii. Endo-enzyme: Enzymes that function inside the cell are called so, e.g. enzymes of glycolysis,
Krebs cycle, protein biosynthesis etc.

iii. Zymogens: These are inactive precursors or pro-enzymes forms of exo-enzymes. They
become activated prior to enzymatic action, e.g., proteases.

iv. Constitute or housekeeping enzymes: Those enzymes are always present and synthesized in
cell, e.g., glycolytic enzymes.

v. Inducible enzymes: Most enzymes are synthesized only when they are needed e.g. Nitric
oxide synthase, cycloxygenase, aldehyde dehydrogenase etc.

vi. Isoenzymes (isozymes): These are the different forms of the same enzymes which catalyze
the same chemical reaction but, differ each other chemically, immunologically, and
electrophoretically and in kinetic properties. For example, in maize 18 isozymes found for
peroxidase. In plants aspertate kinase exist in two isozyme forms. Aspertate kinase catalyzes the
amino acid biosynthesis from aspertate, LDH (Lactic acid dehydrogenase)

vii. Ribozyme or RNA Enzymes: e.g. ribonuclease-P (RNAase-P), Peptidyl transferase (23S
rRNA of larger subunit of ribosome) etc.

viii. Abzymes: These are the antibodies that act as enzymes.

15) Allosteric Sites:

These are special sites on enzyme surface other than catalytic site, which when bind with
effectors or modulators alter the conformation of the catalytic site. The enzymes having allosteric
sites are called allosteric enzymes. Allosteric sites are of two types: activator site and inhibitor
site. An allosteric activator when binds to activator site increase the enzyme activity while an
allosteric inhibitor decreases the enzyme activity by binding the inhibitor site.
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