Enzymesvitamins Full Final

Institute of Chemistry Eötvös Loránd University
Biomolecular Chemistry and Biochemistry
Enzymes and Vitamins – Part I

Enzymes
Fundamentals of General, Organic, and Biological Chemistry
Chapter 19
Main topics of part I

o Catalysis by Enzymes
o Enzyme Cofactors
o Enzyme Classification
o How Enzymes Work
o Factors Affecting Enzyme Activity

Catalysis by Enzymes
What are Enzymes? Biomolecular Chemistry and Biochemistry
o large and complex water-soluble

globular proteins
o catalysts of biochemical reactions:
they decrease reaction time by
lowering activation energy
o breaking existing bonds and forming
new ones
o cannot affect the equilibrium point of
a reaction
o cannot catalyse energetically
unfavorable reactions
Important definitions
o active site: a pocket in an enzyme with the specific
shape and chemical makeup necessary to bind a
substrate
o substrate: a reactant in an enzyme-catalyzed reaction
o specificity: the limitation of the activity of an enzyme

to a specific substrate, specific reaction, or specific
type of reaction
o turnover number: the maximum number of substrate

molecules acted upon by one molecule of enzyme per
unit time
Enzyme Cofactors
Enzyme Cofactors
o to be active, an enzyme may require a
cofactor
o cofactors are either metal ions or non-protein
organic molecules called coenzymes
o cofactors help with extending the limit of
available functional groups in an enzyme
o metal ions from coordinate covalent bonds to
anchor a substrate to the active site of the
enzyme
Cofactor examples Biomolecular Chemistry and Biochemistry
Coenzyme Metal ion
nicotinamide adenine dinucleotide Zn2+

(NAD+)
Enzyme Classification
Nomenclature of Enzymes
There are three methods for naming enzymes:
a) old common naming (e.g. papain is named after papaya)
b) systematic naming (e.g. pyruvate carboxylase)
1) substrate identification
2) enzyme class name
c) name of substrate + „-ase” ending (e.g. fumarase, urease)

I. OXIDOREDUCTASES catalyze oxidation-reduction reactions

II. TRANSFERASES catalyze the transfer of a functional group between two different
compounds
III. HYDROLASES catalyze bond breaking with the addition of water as H and OH to
the fragments
IV. ISOMERASES catalyze the rearrangement of atoms in a substrate

V. LYASES catalyze the addition or elimination of a functional group from a substrate

without hydrolysis
VI. LYGASES catalyze the bonding of two substrate molecules

How Enzymes Work

Models for Enzyme-Substrate Interaction
Lock-and-key model
Induced-fit model
Enzyme-catalyzed reactions
Chymotrypsin
Factors Affecting
Enzyme Activity
Substrate Concentration
o if the substrate concentration is low, not all
enzyme molecules are in use
o initially, the reaction rate is directly

proportional to the substrate concentration,
but it levels off as more active sites are
occupied
o maximum rate: all active sites are occupied

– 108 collisions/mole/liter/second
Enzyme Concentration
o with unlimited substrate concentration,
the reaction rate varies directly with
the enzyme concentration
23
Effect of Temperature on Enzyme Activity
o raising the temperature increases the

reaction rate until a maximum
temperature, then decreases due to the
denaturation of the enzymes
o most enzymes denature above 50-60°C
o cooling does not denature enzymes

Effect of pH on Enzyme Activity
o each enzyme has a well-defined

optimum point at the normal pH of the
enzyme’s environment
o pepsin: pH = 2
o trypsin: pH = 8
o both extremes of pH will denature an

enzyme
Enzymes and Vitamins – Part II

Enzyme Regulation and Vitamins
Fundamentals of General, Organic, and Biological
Chemistry – Chapter 19
Main topics of part II

Enzyme Regulation
Vitamins, Antioxidants and Minerals
o Reversible Uncompetitive
Inhibition o Water Soluble Vitamins
o Reversible Competitve o Fat Soluble Vitamins
Inhibition o Antioxidants
o Irreversible inhibition o Minerals
o Allosteric Control
o Feedback Control
o Covalent Modification
o Genetic Control
27
Enzyme Regulation
28
What is Enzyme Regulation? Biomolecular Chemistry and Biochemistry
o Enzymes can turn some reaction off, slow some down and accelerate others
o Activation: Any process that starts or increases the action of an enzyme
o Inhibition: Any process that slows or stops the action of an enzyme
o These several strategies often operates together
29
Reversible Uncompetitive Inhibition
o Reversible : The inhibitor can leave,

restoring the enzyme to its uninhibited level
o The inhibitor doesn’t compete with the

substrate for the active site
o The inhibitor cannot bind to the enzyme

alone
o The inhibitor binds to the enzyme-substrate

complex
30
Reversible Competitive Inhibition

o Reversible : The inhibitor can leave, restoring
the enzyme to its uninhibited level
o The inhibitor is very similar to the substrate

(size, shape, functional group)
o The inhibitor can enter the active site binding

to it and preventing the substrate from binding
to it
o The effect of the inhibitor depends on the

concentration of the inhibitor and substrate
o Example: lead poisoning

31
Irreversible Inhibition
o Irreversible: the inhibitor cannot

detach from the enzyme
o It accumulates permanently  very
dangerous, especially for children
and pregnant women
o Example: heavy metal poisoning
(mercury and lead ions - covalent
bond to SH group of cysteine)
32
Allosteric Contol
o Binding of a molecule (allosteric regulator) at
one site of an enzyme affects the binding of
another molecule at a different site
o Allosteric enzyme: It’s activity is controlled
by the binding of an activator/inhibitor at a
location different than the active site
o The binding to the enzyme alters the shape
of the active site and enables/disables the
binding of the substrate at the active site
o Negative and Positive allosteric control
33
Feedback Control
o The regulation of an enzyme’s activity by the

product of a reaction later in the pathway
o Occurs when the intermediates are not used in
other metabolic pathways
D is an inhibitor of Enzyme 1
intermediates B and C are
disappearing
34
Covalent Modification
o Removal of covalently bound portion of an enzyme or addition of a group
o Zymogen (proenzyme): Inactive enzyme that becomes active after undergoing a chemical
change
o Example: Digestion of proteins in the small intestine (zymogens are produced in the
pancreas, become active only in the small intestine)
35
Genetic Control
o Regulation of enzyme activity by the

control of the synthesis of enzymes
o Common for enzymes needed only at
certain stages of development
o Example: lactase is not synthesized in
most adults, alcohol dehydrogenase
does not appear in babies
36
1.
Vitamins, Antioxidants
and Minerals
37
Water-Soluble Vitamins
o Vitamins: Organic molecule which is needed for the
function of the body, and not synthetised in the body
o Having polar (–OH, –COOH) goups, making them

water-soluble
o Coenzymes: Vitamin C, Biotin
o Component of a coenzyme: Niacin (B3) in NAD+

pantothenic acid (B5) in coenzyme A
38
Fat-Soluble Vitamins
o Do not have many polar goups

o The molecular mechanism of their
actions are not well understood
o None of them are coenzymes
o They accumulate in body fats 
overdosing can occur
o The Fat-Soluble Vitamins: A, D, E, K
39
Antioxidants
o Antioxidant: substance that prevents

oxidation by reacting with oxidizing agents
o They defuse the action of free radicals
o Example: vitamin C, E, β-carotene, Se
40
Minerals
o Elements, that are used as cofactors,

electrolytes and building blocks for the
human body
o Macrominerals (RDI > 100 mg): Ca, P, K, Cl,
Na, Mg
o Microminerals (RDI < 100 mg): Fe, F, Zn, Cu,
Se, Mn, I, Mo, Cr
41
Thank You For the Attention! :)
Janka Juhász
and
Virág Anik

Questions
o Why is ethanol used for methanol poisoning? Which type of enzyme regulation
mechanism is involved in this case?
o Why is daily ingestion of vitamin C more critical than daily ingestion of vitamin A?
43

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Institute of Chemistry Eötvös Loránd University

Biomolecular Chemistry and Biochemistry

Enzymes and Vitamins – Part I

Main topics of part I

o How Enzymes Work

o Factors Affecting Enzyme Activity

o large and complex water-soluble

o substrate: a reactant in an enzyme-catalyzed reaction

o specificity: the limitation of the activity of an enzyme

o turnover number: the maximum number of substrate

Cofactor examples Biomolecular Chemistry and Biochemistry

Coenzyme Metal ion

nicotinamide adenine dinucleotide Zn2+

There are three methods for naming enzymes:

a) old common naming (e.g. papain is named after papaya)

b) systematic naming (e.g. pyruvate carboxylase)

2) enzyme class name

c) name of substrate + „-ase” ending (e.g. fumarase, urease)

I. OXIDOREDUCTASES catalyze oxidation-reduction reactions

IV. ISOMERASES catalyze the rearrangement of atoms in a substrate

V. LYASES catalyze the addition or elimination of a functional group from a substrate

VI. LYGASES catalyze the bonding of two substrate molecules

How Enzymes Work

o initially, the reaction rate is directly

o maximum rate: all active sites are occupied

Effect of Temperature on Enzyme Activity

o raising the temperature increases the

o most enzymes denature above 50-60°C

o cooling does not denature enzymes

Effect of pH on Enzyme Activity

o each enzyme has a well-defined

o both extremes of pH will denature an

Enzymes and Vitamins – Part II

Main topics of part II

o Activation: Any process that starts or increases the action of an enzyme

o Inhibition: Any process that slows or stops the action of an enzyme

o These several strategies often operates together

Reversible Uncompetitive Inhibition

o Reversible : The inhibitor can leave,

o The inhibitor doesn’t compete with the

o The inhibitor cannot bind to the enzyme

o The inhibitor binds to the enzyme-substrate

Reversible Competitive Inhibition

o The inhibitor is very similar to the substrate

o The inhibitor can enter the active site binding

o The effect of the inhibitor depends on the

o Example: lead poisoning

o Irreversible: the inhibitor cannot

o The regulation of an enzyme’s activity by the

o Removal of covalently bound portion of an enzyme or addition of a group

o Regulation of enzyme activity by the

o Having polar (–OH, –COOH) goups, making them

o Coenzymes: Vitamin C, Biotin

o Component of a coenzyme: Niacin (B3) in NAD+

o Do not have many polar goups

o Antioxidant: substance that prevents

o Elements, that are used as cofactors,

Biomolecular Chemistry and Biochemistry

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