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Enzymes

This document provides a brief introduction to enzymes. It discusses that enzymes are biological catalysts that are proteins found in cells that increase the rates of chemical reactions without being used up in the process. The document then gives a brief history of key discoveries in enzyme research dating back to the 1800s by scientists like Payen, Persoz, Berzelius, Pasteur, Buchner, and Sumner that helped establish our understanding of enzymes. It also outlines the main types of enzymes and how they function to lower activation energy and bring substrates together in the active site for reactions to occur.

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11 views25 pages

Enzymes

This document provides a brief introduction to enzymes. It discusses that enzymes are biological catalysts that are proteins found in cells that increase the rates of chemical reactions without being used up in the process. The document then gives a brief history of key discoveries in enzyme research dating back to the 1800s by scientists like Payen, Persoz, Berzelius, Pasteur, Buchner, and Sumner that helped establish our understanding of enzymes. It also outlines the main types of enzymes and how they function to lower activation energy and bring substrates together in the active site for reactions to occur.

Uploaded by

mainakb2003
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© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Enzymes – A Brief Introduction

LS1101 : Introduction to Biology

Anindita Bhadra

E-mail: [email protected]
What is an Enzyme?

Biological catalyst

Protein in nature

Present in all cells

Increase the rates of chemical reactions

Remain unchanged themselves


A little history

Why is this relevant?

Vessels found in Jiahu village, China,


dating back to 7000 BC

A mixed fermented beverage of rice,


honey, and fruit (hawthorn fruit and/or
grape) was identified.
A little history
Beer production dates back before the
pharaoh, to the Predynastic period (4000-3100
BCE (Before Common Era)), which is the
formative stage of the Egyptian civilization.

Hierakonpolis

Beer was a staple part of their diet and an


essential offering for after life.
A little history

Anselme Payen and Jean-François Persoz extracted the


enzyme diastase from malt solution in 1833.

Greek word: diastasis (a parting, a separation).

In 1836, Berzelius introduced the concept of catalysis.

Wilhelm Kühne coined the term enzyme in 1877.


A little history
During 1856-57, Louis Pasteur studied the
fermentation of sugar to alcohol by yeast.

He concluded that fermentation was catalyzed


by a vital force contained within the yeast cells
called "ferments".

In 1858, he wrote about alcoholic fermentation.

This line of research eventually led to the


discovery of pasteurization.
A little history
Pasteur noted that fermentation requires yeast,
which is living, but does not need oxygen.

His idea was known as “vitalism”.

Justus von Liebig disagreed. He felt vibrations


emanating from the decomposition of organic
matter would spread to the sugar resulting in the
production of carbon dioxide and alcohol.

This was a long-standing dispute.


A little history
In 1897 Eduard Buchner started studying
fermentation.

He created an extract of yeast, and showed that this


could cause fermentation.

He named the enzyme causing fermentation of sucrose


zymase.

This was a blow to the idea of vitalism.


A little history

Note: Buchner had an


interesting early life, and
was not considered to be a
particularly bright student by
his doctoral advisor Adolf
von Baeyer.
A little history
In 1926, James B. Sumner isolated the enzyme
urease from jack beans in pure crystalline form
Enzymes – general features
All enzymes act on specific
substrates

Enzymes have active sites, where


substrates bind.

These active sites are substrate


specific.

Enzymes work by reducing the


activation energy of the reaction.
Enzyme function
Enzyme types

enhance the rate of oxidation and reduction reactions


Oxidoreductases
Eg. - cytochrome oxidase and lactate dehydrogenase.

transfer of groups of atoms, such as methyl (CH3),


Transferases acetyl (CH3CO) or amino (NH2) groups, from one
molecule to another molecule
Eg. - cytochrome oxidase and lactate dehydrogenase.

Accelerate hydrolysis reactions


Hydrolases
Eg. – digestive enzymes lipase and sucrase
Enzyme types
enhance the rate of the addition of one molecular
Lyases group to a double bond or the removal of two groups
from nearby atoms to create a double bond.
Eg. - oxalate decarboxylase and isocitrate lyase.

Speed up isomerization reactions


Isomerases Eg. - glucose-phosphate isomerase and alanine
racemase.

enhance the rate of the joining of two molecules


Ligases
Eg. – acetyl-CoA synthetase and DNA ligase.
Enzyme function

Enzymes lower the activation


energy of reactions.

Enzymes bring reactants


together so they don’t have to
expend energy moving about
until they collide at random.
Enzyme function

By binding reactants at the


active site, enzymes also position
reactants correctly, so they do
not have to overcome
intermolecular forces that would
otherwise push them apart.

Enzymes may also allow


reactions to occur by different
pathways that have lower
activation energy.
Enzyme function

The active site is specific


for the reactants of the
biochemical reaction the
enzyme catalyzes.

The active site is composed of a unique combination of amino acid residues


(side chains or R groups).

A specific chemical substrate matches this site like a jigsaw puzzle piece and
makes the enzyme specific to its substrate.
Enzyme function
Each amino acid residue
can be large or small;
weakly acidic or basic;
hydrophilic or
hydrophobic; and
positively-charged,
negatively-charged, or
The positions, sequences, structures, and neutral.
properties of these residues create a very specific
chemical environment within the active site.
Enzyme function
The activities of enzymes depend on
the temperature, ionic conditions,
and the pH of the surroundings.

The main digestive enzyme in the


stomach is pepsin, which works best
at a pH of about 1.5.

Most biochemical reactions work best


at the normal body temperature of
98.6˚F.
Enzyme function

How do our bodies continue to work


when we have fever?

How do poikilotherms (cold blooded


organisms) function?
The lock-and-key model

This model portrayed the enzyme


as conformationally rigid and able
to bond only to substrates that
exactly fit the active site.
The induced-fit model

Enzymes can undergo a change


in conformation when they bind
substrate molecules, and the
active site has a shape
complementary to that of the
substrate only after the substrate
is bound,
Competitive inhibition

An inhibitor binds to the active


site of the enzyme.

This prevents the substrate from


binding to the enzyme.

So no product is created.
Non competitive inhibition

An inhibitor binds to a secondary


site of the enzyme.

This changes the shape of the


active site, which prevents the
substrate from binding.

So no product is created.

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