INTERNATIONAL UNIVERSITY

SCHOOL OF BIOTECHNOLOGY

ENZYMES- INTRODUCTION,
COENZYME, COFACTORS

LE HONG PHU, ASSOC. PROF. PHD

FUNDAMENTAL BIOCHEMISTRY
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 Learning objectives
1. To realize the enzymes in the real life
2. To know nature of enzyme, structure
and function.
3. To master the properties of enzyme
4. To know the role of coenzymes and
cofactors.

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 Contents

1. WHAT IS ENZYME?
2. PROPERTIES OF ENZYME
3. ACTIVE SITES/ ALLOSTERIC SITES
4. HOW CAN ENZYME WORK?
5. WHAT IS ZYMOGEN?
6. COENZYMES AND COFACTORS

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 Activities
 Students work online to find out 5
names of enzyme that they can be
applied for biotechnology? (5 mins)

 Find out a process where enzyme can

be involved?

 How can enzyme do or work that?

 Find the videos that enzymes can be 4

used?
 1. What is an enzyme?
 The most important functions of
enzyme is their role as catalyst. All
enzymes were considered to be
protein but some examples of RNA
molecules can also be catalyst.
 Living processes consists almost
entirely of biochemical reactions.
Without catalysts these reactions
would not occur fast enough to
sustain life. 5
How a biochemical reaction can happen?

 A reaction happens need the energy to

vibrate the molecules and the reactant
concentration enough. The energy here is
often provided by heat.
 However, in living system, high
temperature may harm the biological
structure
 Truly that the concentration in living
system is very low. So living organisms
solve these problems by using enzyme

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Which properties help enzyme a biocatalyst

1. The rates of enzymatically catalyzed

reactions are often phenomenally
high
2. The enzymes are highly specific to
the reaction
3. Enzyme has the complex structures
so it can be regulated

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 2. Properties of enzymes

 The active site

 Activation energy
 Cofactor

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2. The active site of enzyme:
• The active site takes up a relatively small part of the
total volume of an enzyme
• The active site is a three dimentional entily
• Substrates are bound to enzymes by multiple weak
attraction
• Active sites are clefts or crevices
• The specificity of binding depends on the precisely
defined arrangement of atoms in active site
• Functional residues in enzyme binding directly to
substrate to form or break down the bonding in
substrates to produce products 9
2. Active sites of an enzyme:
- Properties of active sites

+ Many different functional residues of amino acids,

water in bonding, metal ions, functional residues of
coenzyme

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2. Amino acids found in active sites

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2. The active site of enzyme:

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2. The active site of enzyme

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 4. Catalytic mechanism of enzyme
2-phosphoglycerate Enolic intermediate

Phosphoenolpyruvate

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2. The active site of enzyme
Lock and key model (Emil Fischer - 1890)

Induced fit model (Daniel Koshland - 1958)

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2. The active site of enzyme

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 2. Enzyme structure

2. The active site of enzyme:

- Between the active site and substrate, many
weak bonds are formed  easily broken down
during the reaction to release products and
enzyme
- The active site is quaterary level structure

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2. Enzyme structure

Allosteric enzymes
-Active site
- Allosteric site
-Allosteric activators (possitive)
- Allosteric inhibitors (negative)
- Allosteric binding sites

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 2. Enzyme structure
- Allosteric Enzymes:

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 2. Enzyme structure
2. The active site of enzyme:
- Some enzymes exist as the not activated active site zymogens:
pepsinogen, trypsinogen, chymotrypsinogen,...

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Zymogen and the activation of zymogen:
- Zymogen is the state without the enzymatic activity
- Activation of zymogen: zymogen  enzyme , the activation
can be seft-regulated or by some protease

Enzyme catalyzes
Zymogen Enzyme
the activation
Pepsinogen Pepsin Pepsin
Chymotrypsinog Trypsin,
Chymotrypsin
en chymotrypsin
Trypsin,
Trypsinogen Trypsin
enteropeptidase
Procarboxypepti Carboxypeptid
Trypsin
dase ase
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Proelastase Elastase Trypsin
 2. Enzyme structure
Some common features of the activation of Zymogen:

- A hydrolysis to cut one or some bondings at the end –N of

zymogen

- Changing the space structure of zymogen to enzyme

- Productivity of enzyme activation depends on conditions as

to, pH, zymogen concentration, nature of zymogen...

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2. Enzyme structure

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 2. Enzyme structure
2.What is a Coenzyme?
Coenzyme is not protein and its role is to
catalyze a specific kind of reactions

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2. Coenzyme:
Coenzyme is derivatives of Vitamin:

Chemical group(s)
Coenzyme Vitamin
transferred
NAD+ and
Niacin (B3) Electrons
NADP+
Pantothenic acid Acetyl group and
Coenzyme A
(B5) other acyl groups
Methyl, formyl,
Tetrahydrofolic
Folic acid (B9) methylene and
acid
formimino groups
Carbonyl group
Menaquinone Vitamin K
and electrons
Ascorbic acid Vitamin C Electrons
Coenzyme F420 Riboflavin (B2) Electrons 25
Coenzyme is not Vitamin:
Coenzyme Chemical group(s) transferred
Adenosine triphosphate Phosphate group
S-Adenosyl methionine Methyl group
3'-Phosphoadenosine-5'-
Sulfate group
phosphosulfate
Coenzyme Q Electrons
Tetrahydrobiopterin Oxygen atom and electrons
Diacylglycerols and lipid head
Cytidine triphosphate
groups
Nucleotide sugars Monosaccharides
Glutathione Electrons
Coenzyme M Methyl group
Coenzyme B Electrons
Methanofuran Formyl group
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Tetrahydromethanopterin Methyl group
 2. Enzyme structure
2.2. Coenzyme:
- Kinds of coenzymes:
+ Coenzyme of oxido-reduction enzymes : NAD, NADP,
FAD, Ubiquinon,

+ Coenzyme of transport enzymes:

- Coenzyme A, lipoic acid,...
- Biotin, Thiamin pyrophosphate, pyridoxal

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 2. Enzyme structure
2.3. Cofactor:
Helping molecules found in some kinds of enzymes

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ANY QUESTIONS

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Thank you for your kindly listening

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