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Module 3 Lesson 4: Enzymes, Study notes of Biochemistry

Enzymes are biological catalysts made of proteins that speed up chemical reactions in living organisms without being consumed in the process. They work by lowering the activation energy needed for a reaction to occur. Each enzyme has a specific active site that binds to its substrate with high specificity, often described by the "lock and key" or "induced fit" models. Enzymes follow Michaelis-Menten kinetics, characterized by parameters like Vmax (maximum reaction rate) and Km (substrate concentration at half Vmax). They can be regulated through inhibition (competitive, noncompetitive, uncompetitive), allosteric modulation, and covalent modifications (like phosphorylation). Environmental factors such as temperature, pH, and substrate concentration affect enzyme activity. Enzymes play essential roles in metabolism, signal transduction, DNA replication, and many other biological processes.

Typology: Study notes

2022/2023

Available from 05/23/2025

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Enzymes
Biological
catalysts
ooo
°
"
Increased
reaction
rates
-00C
NH
?
Globular
Proteins
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RNA
can
catalyze
reactions
No
binding
-00C
NH
:
Ribozymes
+
ribosomal
RNA
study
of
enzymatic
processes
and
;nr×n
Oldest
field
in
biochem
C-
late
1700
's
)
"
"
¥
,
Coo
-
Coo
-
OH
[
%
.
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hare
Biocatalysts
us
Over
Inorganic
Catalysts
0
Coo
-
Various
potential
pathways
of
[
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reaction
specificity
;
avoids
side
products
decomposition
Kooi
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reaction
conditions
;
conducive
to
conditions
in
cells
Chorismate
COE
¥
"
-00%4
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make
the
desired
pH
-7,37°C
one
most
favorable
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reaction
rates
;
biologically
useful
timeframe
£
"
:
MHz
OH
capacity
for
regulation
;
control
of
biological
pathways
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Catalysts
:
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-
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:
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do
not
affect
equilibrium
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)
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cannot
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free
energy
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)
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,
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of
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-
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entropically
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10
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entropically
unfavorable
¥
P
Conversion
)
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10
'
"
reaction
catalyzed
reactions
orotidine
monophosphate
decarboxylase
/
coordinate
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uses
binding
energy
of
substrates
(
organizes
reactants
-1°
a
fairly
rigid
ES
complex
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active
sites
(
complimentary
-10
transition
state
)
stronger
interactions
with
transition
state
vs
ground
state
Clower
Entropy
cost
(
paid
during
binding
)
activation
)
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reactant
complex
(
entropically
neutral
conversion
)
Largely
AH±
enthalpy
effect
Enzymes
bind
transition
states
best

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Enzymes→^ Biological^ catalysts

ooo^ →

  • Increased^ reaction rates

-00C (^) NH? Globular Proteins

¥¥H|

  • RNA can (^) catalyze reactions

-00C →^ No^ binding

NH: • Ribozymes + ribosomal RNA

study of^ enzymatic processes → and (^) ;n◦r×n " (^) " • Oldest^ field in biochem^ C- late^1700 's)

Coo- Coo^ - OH (^) [ %. Metabolites hare Biocatalysts us^ Over^ Inorganic^ Catalysts^0 Coo^ -^ Various^ potential

[^ pathways^ of

Greater reaction (^) specificity ; avoids side^ products decomposition Milder reaction^ conditions^ ; conducive^ to^ conditions^ in^ cells^ Kooi

Chorismate COE

" -00%4 Enzymes^ make^ the^ desired

pH -7,37°C^ • one^ most^ favorable

Faster (^) reaction rates (^) ; (^) biologically useful timeframe^

MHz OH capacity for^ regulation ;^ control^ of^ biological^ pathways Enzymatic Catalysts : Enzyme -^ Substrate^ Complex :^ Selectivity Enzymes do^ not^ affect^ equilibrium^ Ikea) Enzymes cannot^ affect^ free^ energy IAG) Bf ~ ygμgμ, gmym.mang.ggna.egqgp.a.ggslightly as substrate ,

lGM⑨U

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( G- ± )); surmounted

e-

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substrate entering Enzyme/ Enzyme/

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state unfavorable conversion

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" flexible reactant →

rigid transition^ State^ (entropically unfavorable ¥ P Conversion) Urease 10 '^ " reaction catalyzed^ reactions orotidine monophosphate decarboxylase /^ coordinate Enzyme uses (^) binding energy of substrates (organizes reactants^ -1° a (^) fairly rigid ES^ complex Enzyme active^ sites^ (complimentary^ -10^ transition^ state) stronger interactions^ with^ transition^ state^ vs^ ground^ state^ Clower^ Entropy^ cost (paid (^) during binding) activation) Rigid^ reactant^ complex^ →^ (entropically^ neutral^ conversion) Largely AH±^ enthalpy effect^ Enzymes^ bind^ transition^ states^ best