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dr. Santoso
A.Introduction
B. Mechanisms of Enzymatic reaction
C. Factor affecting enzyme activity
D.Regulation of enzyme activity
A.Introduction
B. Mechanisms of Enzymatic reaction
C. Factor affecting enzyme activity
D.Regulation of enzyme activity
Enzymes
A.Introduction
B. Mechanisms of Enzymatic reaction
C. Factor affecting enzyme activity
D.Regulation of enzyme activity
Enzyme-Substrate Complex
The substance
(reactant) an
enzyme acts on is
the substrate
Substrate
Joins
Enzyme
11
Active Site
Enzyme
12
S1
enzyme
Products
P P
enzyme
ENZYME SUBSTRATE
COMPLEX
Induced Fit
A change in the
shape of an
enzymes active
site
Induced by the
substrate
14
Induced Fit
A change in the configuration of an
enzymes active site (H+ and ionic
bonds are involved).
Induced by the substrate.
substrate
Active Site
Enzyme
induced fit
15
Enzyme Cooperativity
Some enzymes have
multiple active site. It
has been observed that
when one substrate
molecule binds to a
single active site in the
inactive form or tense
state of the enzyme, a
configurational change
occurs in the other
active sites making them
more receptive to other
substrate molecules.
A.Introduction
B. Mechanisms of Enzymatic reaction
C. Kinetic of enzyme activity
D.Factor affecting enzyme activity
E. Regulation of enzyme activity
Enzyme Kinetics
Expression for enzyme catalyzed reaction:
E+S
k1
k-1
ES
k2
E+P
Michaelis-Menten Equation
V0 = Vmax[S] / KM + [S]
Rate increase with [S]
Rate levels off as
approach Vmax
More S than active
sites in E
Adding S has no effect
A.Introduction
B. Mechanisms of Enzymatic reaction
C. Factor affecting enzyme activity
D.Regulation of enzyme activity
22
1. Environmental Conditions
1. Extreme Temperature are the most
dangerous
high temps may denature (unfold)
the enzyme.
2. pH (most like 6 - 8 pH near neutral)
3. Ionic concentration (salt ions)
23
Temperature
All enzymes have an
optimum temperature at
which they work best.
If you observe the
enzymes activity below
the specific
temperature it will
steadily increase until it
reaches the optimum.
After the optimum
temperature is reached
the enzymes activity
drops dramatically due
to denaturing.
pH
All enzymes have an
optimum pH at which
they work best. If
the pH falls below or
rises above the
optimum value,
enzymatic activity
decreases
as a result of
denaturing.
Substrate Concentration
The concentration of substrate also has an affect on the rate
of enzyme activity. If the concentration of substrate is
increased while the concentration of enzyme is constant, the
level of enzyme activity will increase until a point of saturation
is reached. At this point there are no enzymes available to
react with excess substrate and the rate of the reaction
stabilizes. No matter if you continue to add substrate, the
reaction rate will not increase!
Rate of Reaction
pick
27
Coenzyme
Deficiency
Thiamine (B1)
Thiamine
pyrophosphate
Beriberi (weight
loss,other problems
Riboflavin (B2)
FAD+
Nicotinic acid
(niacine)
NAD+
Pellagra (dermatitis,
depression)
Pantohtinic acid
Coenzyme A
Hypertension
Biotin
Biotin
3. Enzyme Inhibitors
Competitive inhibitors
chemicals that resemble an enzymes
normal substrate and compete with
it for the active site.
site
Substrate
Competitive inhibitor
Enzyme
31
Noncompetitive Inhibitors
Inhibitors that do not enter the active site,
site but
bind to another part of the enzyme causing the
enzyme to change its shape,
shape which in turn
alters the active site.
site
Substrate
active site
altered
Enzyme
Noncompetitive
Inhibitor
32
A.Introduction
B. Mechanisms of Enzymatic reaction
C. Factor affecting enzyme activity
D.Regulation of enzyme activity
Allosteric control
Covalent modification
Proteolytic activation
Stimulation and inhibition by control proteins
Allosteric regulation
Enzyme
Inactive Enzyme
Modifying
group
Enzyme
Active Enzyme
O
O P O
O-
Proteolytic activation
Proteolytic activation
.
(inactive)
Propeptide
P ro p e p tid e
Enzyme
Enzyme
(active)
Proteolytic
Enzyme
Val
(Asp)4 Lys +
Ile Val
Trypsin
Proteolytic activation
of digestive enzymes
pepsinogen
(inactive)
Secretion into
stomach (pH 2)
autocatalytic
cleavage of
pepsinogen after
amino acid 44
pepsin
(active)
Zymogen
Active Enzyme
Function
Pepsinogen
Chymotrypsinogen
Trypsinogen
Procarboxypeptidase
Proelastase
Prothrombin
Fibrinogen
Factor VII
Factor X
Proinsulin
Procollagen
Procollagenase
Pepsin
Chymotrypsin
Trypsin
Carboxypeptidase
Elastase
Thrombin
Fibrin
Factor VIIa
Factor Xa
Insulin
Collagen
Collagenase
protein digestion
protein digestion
protein digestion
protein digestion
protein digestion
blood clot formation
blood clot formation
blood clot formation
blood clot formation
plasma glucose
homeostasis
component of skin and
bone remodeling
processes during
metamorphosis, etc.
XII
XIIa
Extrinsic Pathway
Trauma
XIa
XI
VII
VIIa
Tissue
IXa
VIIIa factor
IX
Xa
Va
Prothrombin
Thrombin
Fibrinogen
Fibrin
XIIIa
Cross-linked
fibrin clot
Enzyme
(inactive)
Inhibitory
Protein
3. Proteolytic activation
Digestive enzyme, blood clotting factors
Feedback inhibition
Many enzymes are actually regulated by the
end products of the reaction they catalyze
Start of
pathway
Enzyme 1
Intermediate
Enzyme 2
Intermediate
Enzyme 3
Product
Klasifikasi Enzim
Sistem Penamaan Enzim
Spesifitas Enzim
Macam-macam Bentuk Enzim
Klasifikasi Enzim
5 kelas
Oksidoreductase
Transferase
Hidrolase
Isomerase
Ligase
Spesifitas Enzim
Enzim biasanya sangat spesifik dalam aksinya.
Beberapa kespesifikan yang dimiliki oleh enzim antara lain :
Kespesifikan
Kespesifikan
Kespesifikan
Kespesifikan
geometrik
reaksi
optik.
organella
Enzim plasma
fungsional
fungsional
Konsentrasi Lebih
tinggi
dalam Secara normal, konsentrasi
dalam
plasma
dibandingkan di
plasma
dengan dijaringan
dalam
plasma
sangat
Fungsi
Jelas
Tidak jelas
Substrat
Tempat
Hepar
Diberbagai
macam
organ
sintesis
Contoh
Factor pembekuan
Lipoprotein lipase
phospatase, amilase
Pseudocholine
esterase
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