BIOLOGY I QUARTER

ENZYME
NOVEEH NHASTASCY S.
ATCHUELA
 Enzymes are protein
macromolecules.
What is  They have a defined amino acid sequence, and
Enzyme? are typically 100-500 amino acids long.
 They have a defined three-dimensional
structure.
 Enzymes are proteins that function as
catalysts.
This means they help to speed up chemical
reactions
How? They lower the activation energy of
Function reaction so it takes LESS energy for the reaction
to take place.
of Enzyme Enzymes are very specific and will only catalyze
one specific chemical reaction. This means
there are TONS of enzymes at work at all times!
Enzymes are reusable. Once an enzyme
binds to a substrate and catalyzes the
reaction, the enzyme is released, unchanged,
and can be used for another reaction.
Enzymes Lower a
Reaction’s
Activation Energy

All chemical reactions

require some amount of
energy to get them
started.
OR
It is First push to start
reaction.

This energy is called

activation energy.
 Structure of Enzymes
Enzymes match
with a substrate
Substrate that fits like a
puzzle at an
STRUCTU Active active site.

RE OF Site
ENZYME
Enzyme
 Structure of Enzymes
Enzymes match
with a substrate
that fits like a
puzzle at an
active site.
STRUCTU
RE OF
ENZYME
  The structure of enzymes and substrates are a “lock and
key” model
 The molecules that bind to the enzyme are called
substrates.
 The location where they bind (sit down) is called the
active site.

STRUCTU
RE OF 1
2 3

ENZYME
• After the enzyme and substrate bind it is called an
enzyme-substrate complex.
• The substrate may break apart or bond together to form
a product.
  Typically add “-ase” to name of substrate
 e.g. lactase breaks down lactose (dissacharide of glucose and
galactose)
 Enzymes based upon the class of organic chemical reaction
catalyzed:
1. Oxidoreductase - catalyze redox reactions; dehydrogenases,
NOMENCLAT oxidases, peroxidases, reductases.

URE 2. Transferases - catalyze group transfer reactions; often require

coenzymes.
3. Hydrolases - catalyze hydrolysis reactions.
4. Lyases - lysis of substrate; produce contains double bond.
5. Isomerases - catalyze structural changes; isomerization. 6.
Ligases - ligation or joining of two substrates with input of energy,
usually from ATP hydrolysis; often called synthetases or synthases.
 Lipase — breaking down of fats (lipid)
Protease — breaking down of proteins
Cellulase — breaking down of fiber (cellulose)
Examples of Amylase — breaking down of starch (amylose)
biological Lactase — breaking down of dairy products (lactose)

enzymes Sucrase — breaking down of sugar (sucrose)

Maltase — breaking down of grains (maltose)
 ENZYME
COMPONE
NTS
 ENZYME
COMPONE
NTS
  Apoenzyme:
 is an inactive enzyme, activation of the enzyme
occurs upon binding of an organic or inorganic
cofactor.
 are enzymes that lack their necessary cofactor(s)
ENZYME for proper functioning

COMPONE a Protein

NTS
  Holoenzyme:
• are the active forms of apoenzymes.
(Apoenzyme plus cofactor)
• DNA polymerase and RNA polymerase are
ENZYME examples.
COMPONE
NTS
  Cofactor:
 mostly metal ions or small organic molecules,
are inorganic and organic chemicals that assist
enzymes during the catalysis of reactions. •
ENZYME Nonprotein component (e.g. magnesium, zinc
COMPONE
NTS
  Coenzyme:
are non-protein organic molecules that are
mostly derivatives of vitamins soluble in water
by phosphorylation
ENZYME  Organic cofactor (Eg: NADH, FADH)
COMPONE
NTS

Many enzymes can catalyze a reaction only if coenzymes, or cofactors are present