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1.Oxidoreductase
O
CH3 -C- COO - + NADH + H
Pyruvate
lactate
deh ydrogenase
OH
+
CH 3 -CH -COO - + NAD
Lactate
2.Transferase
COOCH2
CH- NH3 +
COO-
COOAspartate amino
C= O
transfer ase
CH2
COOCH2
C= O
CH2
COO-
COOAspartate -Ketoglutarate
COOC-NH3 +
CH2
CH2
COO-
Oxalosuc cinate
G lutamate
3.Hydrolase
O
CH3 -C- OCH 2 CH 2 N( CH3 ) 2 + H O Acetylcholinesterease
2
Acetylcholine
O
CH3 -C- O-
Ace tate
Choline
COOCH2
C-COO - + H O
2
CH
COOcis- Aconitate
4. Lyase
Aconitase
5. Isomerase
COOCH2
C-COO HO C-H
COOIsocitrate
6. Ligase
ATP + L -tyros ine + t-RNA
Ty ros ine-tRNA
s yntheta se
Substrate of an
enzyme are the
reactants that are
activated by the
enzyme
E
E
E
Enzymesubstrate
complex
Enzyme may
be used again
P
Reaction coordinate
Fit between the substrate (key) and the active site of the enzyme
(lock) is very precise
Temporary structure called the enzyme-substrate complex
formed
Products have a different shape from the substrate
Once formed, they are released from the active site
Leaving it free to become attached to another substrate
substrate concentration
pH
temperature
inhibitors
Reaction
velocity
Substrate concentration
Vmax
Reaction
velocity
Substrate concentration
A linear curve
A saturation curve
At constant substrate
concentration, increasing the
enzyme concentration,
increases the rate linearly.
(In practically all enzyme
reactions, the molar conc. of
enzyme is always much lower
than that of substrate.)
At constant enzyme
concentration, increasing the
substrate concentration does
not increases the rate
continuously. A saturation
point is achieved.
The effect of pH
Extreme pH levels will produce denaturation
The structure of the enzyme is changed
The active site is distorted and the substrate
molecules will no longer fit in it
At pH values slightly different from the enzymes
optimum value, small changes in the charges of
the enzyme and its substrate molecules will
occur
This change in ionisation will affect the binding
of the substrate with the active site.
Q10
Enzyme
activity
10
20
30
40
Temperature / C
Denaturation
50
E1
E2
E3
Inhibitors
E+I
Reversible
reaction
EI
Enzyme inhibitor
complex
inhibitors.
Maximum reaction rate
is the same without an
inhibitor and in the
presence of a
competitive inhibitor
(CI).
Maximum rate is
obtained at high
substrate concentration
for CI but low with no
inhibitor.
If the inhibitor is non
competitive, the
maximum rate of
reaction is lower.