Enzym dan hormon

Enzymes and Hormones

• Enzymes allow chemical reactions of metabolism to occur at rates
sufficient to maintain normal body function
• Coenzymes assist enzymes
Enzymes
• Enzymes: molecules that catalyze - speed up - biochemical reactions
in living cells

• Three rules to be considered an enzyme

• Most are proteins (some RNA enzymes)
• Lower the energy of activation required for a reaction to occur
• Are not changed or consumed by the reaction

• Cofactors, Coenzymes

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Metabolism

 Enzymes catalyze cellular chemical reactions

 Metabolism - the chemical reactions in a cell:
 Two categories of cellular chemical reactions:
1.Anabolic Reactions
 Build larger molecules for growth, repair, reproduction
 Dehydration Synthesis Reactions
 require energy and nutrients
2.Catabolic Reactions
 Breakdown larger molecules
 Hydrolysis Reactions
 mobilize nutrients for energy making it available to the cell

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Metabolism

 Metabolism is the sum total of all anabolic and catabolic reactions

that occur in the cell
 The metabolism of cells is carried out and controlled by the enzymes
• There are catabolic enzymes – those that cleave larger molecules into
smaller ones
 Ex. Hydrolysis Reactions
• There are also anabolic enzymes – those that assemble smaller molecules
into larger ones
 Ex. Dehydration Reactions

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Enzymes
• Enzymes interact with substrates.
• substrate: molecule that will undergo a reaction
• active site: region of the enzyme that binds to the
substrate

• Binding of an enzyme to a substrate causes the

enzyme to change shape, producing a better induced fit
between the molecules.

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Enzymes
Enzymes interact with substrates
Substrates: molecules that will undergo a reaction when bound to the
enzyme
• lactose, hydrogen peroxide (H2O2)

On the Enzymes:

• Active site: region of the enzyme that binds to the substrate
• Allosteric site: region of the enzyme that binds substances other that the
substrate

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Figure 5_02
Enzymes
 Enzymes are very specific:
• Enzymes will only interact with a specific substrates
• The substrate fits into the active site like a key fits into a lock (Lock and Key
Hypothesis)
• Substrate binding causes the enzyme to change shape, producing a better
induced fit between the molecules (Induced Fit Hypothesis)

 Changing the shape of an enzyme affects its ability to function

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Enzymes

 Enzyme/Substrate Complex:

E+S ES EP E+P
1.The Enzyme and the Substrate come together (E+S)
2.The Enzyme/Substrate Complex is formed (ES)
3.The Enzyme’s Substrate is changed to the Enzyme’s
- Product in the active site of the enzyme (EP)
4.The Enzyme and Product Separate (E+P)
5.The Enzyme is free to bind to another Substrate

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Figure 5_03b
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Enzyme Naming Convention
 Because enzymes catalyze specific reactions each enzyme has a unique name:
• The first part of an enzyme’s name usually describes the substrate
• The second part of an enzyme’s usually indicates the type of reaction it will
catalyze
 Most enzyme names end in the suffix -ase
 Examples of enzymes:
• DNA polymerase
• Glycogen synthetase
• Lactase
• Catalase

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How Enzymes Work
 Enzymes lower the activation energy of biochemical reactions.
 Enzymes make it easier for chemical reactions to occur:
– by destabilizing the bonds in the substrate
– by bringing substrates together so they react
– by decreasing entropy - disorder - in the system
 Enzymes make the chemical reactions possible in the cell’s
environment
 Enzymes make cells very efficient

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How Enzymes Work

Enzymes make cells very efficient

Through enzymes, cells can carry out anabolic
and catabolic reactions and end up with a net
profit of energy
Cellular respiration is the process of breaking
down glucose and storing the excess energy
from the molecule into a form of energy that is
available and useful to the cell

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Cells Use Enzymes to Process Energy and
Matter
 Reactions that break
chemical bonds release
their internal potential
energy.
– Example: burning wood
– Oxidation reactions

• Organisms obtain energy

through enzyme-
catalyzed biochemical
reactions.

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Coenzymes and Cofactors
 Many enzymes require special molecules to help
them function correctly:
• Cofactors
• inorganic molecules ions, such as zinc or iron
• Coenzymes
• organic molecules

 Vitamins are the precursors for many coenzymes.

 Vitamins must
be acquired from the diet, cells
cannot make them.

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The Role of Coenzymes

• ADase oxidizes alcohol

- Alcohol cannot be oxidized unless
something else is reduced
- NAD+ is reduced to NADH

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The Environment Affects
Enzyme Function
 The rate at which an enzyme can bind to a substrate is called the turnover
number.
 The turnover number is maximized under the ideal conditions for that
enzyme.
 Conditions that can change an enzyme’s 3-dimensional shape can change
its function
 Each enzyme has ideal conditions that include:
1.Temperature
2.pH
3.Substrate concentration
4. Regulatory molecules
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1. Temperature
 Temperature has two effects on enzymes:
• Changes the rate of molecular motion
1. Increasing temperature increases molecular motion and increases
turnover number
2. Decreasing temperature decreases molecular movement and
decreases turnover number

• Causes changes in the shape of an enzyme

 Temperature changes above optimum will denature the enzyme.
 This changes its shape, and it can no longer bind substrate and
catalyze the reaction.

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2. pH
 Enzymes are composed of amino acids
• In a basic environment
 The acidic side chains (R groups) could donate protons which affects the charge of the
side chain
 A neutral side chain that donates protons would become negatively charged

• In an acidic environment
 The basic side chains (R groups) could accept protons which affects the charge of the
side chain
 A neutral side chain that accepts protons would become positively charged

 Both of these events can change the enzyme’s shape

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Enzymes
• Enzymes work together in chains of reactions known
as biochemical or metabolic pathways

• Biochemical pathways are a series of reactions in

which the product of one reaction becomes the
substrate for the next reaction.

• Examples: photosynthesis, cellular respiration,

protein synthesis, etc.

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Metabolic Pathways
• Metabolic Pathways are series of chemical reactions
carried out by separate enzymes

• It is a sequence of chemical reactions where each

reaction is controlled by a separate enzyme

• The product of one enzyme serves as the substrate for

the enzyme of subsequent reaction in the metabolic
pathway
Enzymes

• These biochemical pathways offer certain advantages:

1.The product of one reaction can be directly delivered to the
next enzyme
2.The possibility of unwanted side reactions is eliminated
3. All of the reactions can be regulated

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Regulation of Biochemical Pathways

 Metabolism is tightly regulated

 There is a delicate balance between all of the
reactions that take place in the cell
 Metabolism is commonly regulated 3 ways:
1.Enzymatic competition for substrate
2.Gene regulation
3.Enzyme inhibition

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Enzyme Regulation

1. Enzymatic competition for substrate

Enzymatic competition occurs when more than one
enzyme interacts with the same substrate

Each enzyme converts the substrate to a different product.

Theenzyme that “wins” is the one that is the most
abundant at the time.

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Figure 5_07
Enzyme Regulation

2. Gene regulation
Enzymes are proteins.
Protein production is controlled by genes.
Certain chemicals in the cell turn particular enzyme-
producing genes on or off depending on the situation.
• Called gene-regulator proteins
 Those that decrease the amount of an enzyme made are called
gene-repressor proteins.
 Those that increase the amount of an enzyme made are called
gene-activator proteins.

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Enzyme Regulation
3. Enzyme inhibition
•Inhibitors are molecules that attach to enzymes and make them unable to bind to
substrate.
•Many drugs, pesticides and herbicides target enzymes.
•Three types of inhibition:
A. Negative Feedback Inhibition
B. Competitive Inhibition
C. Noncompetitive Inhibition

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A. Negative-Feedback Inhibition

 The end-product of the metabolic pathways accumulate

• Those molecules feedback and bind to an enzyme
early in the sequence.
• They inhibit that enzyme, and stop the sequence.
• This decreases the amount of end-product made.

 This functions to keep levels of the end-product within a

certain range.

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Feedback Inhibition

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Text art 5_05
Enzyme Regulation
• Inhibitors are molecules that bind to an enzyme to decrease enzyme
activity.
- competitive inhibitors compete with the substrate for binding to the same
active site

- noncompetitive inhibitors bind to sites other than the enzyme’s active site

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B. Competitive Inhibition

 Competitive inhibitors
closely resemble the
substrate.
• they bind to the active
site of the enzyme and
block the substrate
from binding.

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Figure 5_09
Enzyme Regulation
• Allosteric enzymes exist in either an active or inactive state.
- possess an allosteric site where molecules other than the substrate bind
- allosteric inhibitors bind to the allosteric site to inactivate the enzyme
- allosteric activators bind to the allosteric site to activate the enzyme

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C. Noncompetitive Inhibition
 Noncompetitive inhibitors bind to sites other than the enzyme’s
active site - allosteric sites
 “allo” = other; “steric” = shape
• binding to an allosteric site changes the shape of the enzyme and affects its
function

 Noncompetitive because the noncompetitive inhibitor does not

compete with the substrate to bind to the active site

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