Historical facts

1
Historical facts

• 1835 Berzelius J.J. Theory of chemical catalyst
• 1860 Pasteur L. yeast, catalyst boud to cells
• 1899 Buchner E. Isolation of enzymes of
  alcoholic fermentation
• 1926 Summer B.J. Preparation of plant urease in
  crystalline form
• 1930-1936 Northrop Isolation of pepsin, trypsin
  and chymotrypsin in crystalline form
• Az enzimek proteins (99,9)?

2
Enzymes

• Biochemical, physiological role
• Regulation of the enzyme activity
• Therapy
• Their clinical role

3
Chemical kinetics

• Classification of chemical reaction
• Molecularity mono-, bi-, termolecular reactions
• Order of reaction zero-, first-, second-,
  thirdorder

4
Reactions of first-order
k rate constant, s-1
5
Reaction of second order
6
Reactions of pseudo-first order
A gtgt B A ltlt B
7
Catalyst
8
?G K
Exergon spontaneously, ?Glt0 Kgt1 Endergon ?G gt0
Klt1
9
Enzymes Common in mode of action
Enzyme substrate binding side
Substrate
Active site
10
Enzyme activity influence of temperature
Ac
t oC

• Increase in temperature increase of activity
• Increase in temperature heat denaturation

11
Enzymes pH optimum
trypsin
Cholinesterase
pepsin
papain
Activity
pH 8
pH 8
pH 2
pH 6
12
Michaelis-Menten kinetics
KM
13
Michaelis Menten kinetics
Vmax
vo
Vmax/2
Subsztrate Enzyme
KM
Substrate M
14
Michaelis Menten kinetics
15
Michaelis Menten kinetics
Rate of enzyme-substrate complex formation
16
Michaelis-Menten kinetics
Rate of degradation of enzyme substrate complex
17
Michaelis-Menten kinetics
Stationary state (Steady state)
18
Michaelis-Menten kinetics
C
Time
19
Michaelis-Menten kinetics
v k3 ES
20
Michaelis-Menten kinetics
21
Michaelis-Menten kinetics
vo
Substrate M
22
Michaelis-Menten kinetics
23
Asparaginase enzyme activity
Km
24
Michaelis-Menten kinetics
25
Lineweaver-Burk plot
a KM/VMax
1/v
1/VMax
1/S
-1/KM
26
Lineweaver-Burk plot