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Enzymes Lecture

1. Enzymes are protein catalysts that speed up biochemical reactions. They have an active site that substrates fit into to undergo reactions. 2. Isoenzymes are different forms of the same enzyme that catalyze the same reaction in different parts of the body and can be used for medical diagnosis. 3. Enzyme activity is affected by temperature, pH, substrate concentration, and inhibitors. Diagnostic tests often measure enzyme levels or function to assess organ health.

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52 views

Enzymes Lecture

1. Enzymes are protein catalysts that speed up biochemical reactions. They have an active site that substrates fit into to undergo reactions. 2. Isoenzymes are different forms of the same enzyme that catalyze the same reaction in different parts of the body and can be used for medical diagnosis. 3. Enzyme activity is affected by temperature, pH, substrate concentration, and inhibitors. Diagnostic tests often measure enzyme levels or function to assess organ health.

Uploaded by

glenn johnston
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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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Session One Part 2

 Textbook reference:
 Chapter 16, Sections 16.6-16.9.

 Definition:
 Act as “biological catalysts”
 Protein based
 Have an active site where reactions occur

2
 Active site:
 Region within enzyme where reactant or substrate fits
to facilitate enzymatic catalysis (see Figure 16.15, page
547).
 Substrate can fit into active site by either “lock and key”
or ”induced fit” mechanisms - both are highly
specific.
 Isoenzyme:
 Different form of same enzyme that catalyses the
same reaction in different parts of the body.
 Useful for diagnosis of the type of organ affected
 E.g. isoenzyme released from heart will be different to those of
the kidneys, thus indicating a myocardial infarct. 3
E+S  ES  EP  E + P

P
S S P

E E

E E

E + S  ES  EP  E + P
4
Activity of enzymes is affected by:
 Temperature:
 Enzymes have an optimal functional temperature (37oC);
at > 37oC they are sluggish and at < 50oC they are
denatured.
 pH:
 Enzymes have an optimal functional pH; mostly 7.4,
but some function best at other pHs.
 Concentration:
 increasing substrate concentration increases enzyme
activity, as long as there are more enzymes than
substrate particles around (I.e: saturation).
 Inhibitors:
 Affect enzyme activity chemically.
5
 To determine how well an organ or tissue is
functioning many diagnostic tests rely on
enzyme assays:
1. Enzyme function assays:
– Determines whether an enzyme functions
adequately
– A known amount of labeled substrate is
administered to the patient and the amount of
product produced is analysed.
2. :

3. Enzyme level assays:


– Assesses amount of enzyme in tissue
– Healthy tissue contains a known amount of a certain
enzyme
– If tissue is diseased, the levels of enzyme will be
elevated.
6
 Competitive inhibition:
 Inhibitor binds directly into same active site that
substrate fits into, thus stopping catalysis of the
reaction. Sometimes the product acts as a
competitive inhibitor intentionally in the body to
control reaction rate.
 E.g. antibiotics. Penicillin is an enzyme needed by bacteria
to form cell walls (but not by human cells)

 Non-competitive inhibition:
 Inhibitor binds somewhere else on the enzyme (not
the active site) and distorts the shape of the enzyme
so the substrate doesn’t fit into the active site any
more, thus stopping catalysis of the reaction.
 Heavy metal poisoning (Pb, Ag, Hg) and antibiotics
work this way.
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 Enzymes cannot participate in the reaction
occurring between a substrate and a product
 Enzymes DO NOT CHANGE.
 Enzymes need cofactors or coenzymes for
the reactions to occur.
 There are two types of coenzymes:
 Cofactors (Table 16.12)
 Non-protein atoms (usually metal ions) required by
some enzymes to catalyze reactions (e.g: Cu2+, Mg2+,
Zn2+). Mainly derived from minerals in our diets.
 Coenzymes (Table 16.13)
 Non-protein organic molecules (usually vitamins)
required by some enzymes to catalyze reactions (e.g:
vitamins B1, B2, C, biotin).
 Mainly derived from vitamins in our diets.
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1. Nicotinamide adenine dinucleotide
 A.k.a. NAD+

2. Flavin adenine dinucleotide


 A.k.a. FAD

3. Co-enzyme A
 A.k.a. CoA

9
10
 Made from niacin (nicotinamide- B3) bonded to
adenosine diphosphate (ADP).
 Picks up two electrons and H+ (equ. hydride ion) and
becomes reduced to NADH
 E.g. the oxidation of alcohol
 Glycolysis and Krebs cycle
 This reaction produces a carbon-oxygen double
bond: C=O.
O
Alcohol
dehydrogenase
CH3 - CH2 - OH + NAD+  CH3 - C- H + NADH + H+

Ethanol Acetaldehyde

11
 Acetaldehyde is
believed to cause
hangovers.
 The drug disulfiram
(Antabuse) prevents the
oxidation of
acetaldehyde to acetic
acid, and it has the same
unpleasant effect on
drinkers.
 Antabuse is used as a
deterrent for alcoholics
who wish to stay sober.

12
 Made from riboflavin (B2) bonded to adenosine
diphosphate (ADP) moiety.
 Picks up two hydrogen atoms H+ (a net gain of two
electrons) and becomes reduced to FADH2
 E.g. the oxidation of alcohol
 This reaction produces a carbon-carbon double bond
(C=C).

H H

FAD + R - C - C - R  R - C = C - R + FADH2

H H H H

Oxidised Reduced Oxidised Reduced 13


 FAD is fundamentally
involved in the
production of ATP via
the Krebs cycle (step
8).
 It carriers electrons to
the electron transport
chain.

14
 The universal carrier of acyl groups (2C units).
 Made from panthothenic acid (vitamin B5) bonded
to adenosine diphosphate (ADP) and
aminoethanethiol.
 This co-enzyme contains sulfur (sulfhydryl) and
reacts with acyl groups (an RCO- group whereby
C=O is a double-bond).
 Conversion of pyruvate (C3H3O3) to Acetyl CoA-
during this process CoA accepts the acetyl group.
O O

CH3 - C - R + HS - CoA  CH3- C - S - CoA

Pyruvate (glycolysis) Acetyl CoA (Krebs Cycle)


15
 Ultimately the reduced forms of these electron
carriers donate there high-potential electrons to
oxygen.

This reaction is coupled with the reformation of ATP


from ADP by a process known as oxidative
phosphorlyation.

16

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