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Bio 1 Enzym
Bio 1 Enzym
Cofactor
Prosthetic group : very tightly or even covalently bound to
enzyme (covalently bound)
Classification of enzymes
IUB:
- Each enzyme has a unique name and code number that reflect the type of
reaction catalyzed and the substrate involved.
- EC 1.2.3.4
- EC, Enzyme catalog
- 1, Class
- 2, subclasses
- 3, subsubclasses
- 4, where the enzyme belongs in the subsubclases.
- EC 2.7.1.1
- class 2, transferase
- subclass 7, transfer of a phosphoryl group.
- subsubclass 1, alcohol is the phosphoryl acceptor.
- 1, hexose-6, alcohol phosphorylated is the of carbon-6 of a hexose.
Enzyme Classes (IUB)
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5. How enzymes work (important!)
1) Enzymes lower a
reactions activation
energy
All chemical reactions have
an energy barrier, called the
activation energy,
separating the reactants and
the products.
activation energy: amount
of energy needed to disrupt
stable molecule so that
reaction can take place.
Enzymes
Lower a
Reactions
Activation
Energy
What is the difference between an
enzyme and a protein?
Binding site
Active site
Catalytic site
The Lock and Key Hypothesis
S
E
E
E
Reaction coordinate
2007 Paul Billiet ODWS
The Lock and Key Hypothesis
This explains enzyme specificity
This explains the loss of activity when enzymes
denature
http://en.wikipedia.org/wiki/File:Induced_fit_diagram.svg
Life Sciences-HHMI Outreach. Copyright 2009 President and Fellows of Harvard College
The Induced Fit Hypothesis
Vomax [S]
Vo= ----------
Km + [S]
Apabila
[S] <<< Km
[S] >>> Km
[S] = Km
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(2) Effect of [E] on velocity
[S]>>[E] V[E]
The initial rate of an
enzyme-catalyzed
reaction is always
proportionate to the
concentration of enzyme.
This property of enzyme
is made use in
determining the serum
enzyme for the diagnosis
of diseases.
(3) Effect of temperature on
velocity Bell-shaped curve
(4) Effect of pH value on velocity
Bell-shaped curve
Each enzyme has
an optimal pH or pH
range (where the
enzyme has maximal
activity).
Requirements for
the catalytic groups
in the active site in
appropriate
ionization state is a
The pH optimum varies for different
enzymes.
common reason for
Most enzyme: neutral pH (6-8). this phenomenon.
The effect of pH
Optimum pH values
Enzyme
activity Trypsin
Pepsin
1 3 5 7 9 11
(ii). Organic
Reducing agents, such as CysGSH
(iii). Proteins
(6) Inhibition of enzyme activities
(very important!)
Inhibitor: any molecule which acts
directly on an enzyme to lower its
catalytic rate is called an
inhibitor.(not denaturation)
Some enzyme inhibitors are normal
body metabolites.
Other may be foreign
substances,such as drugs or toxins.
8. REGULATION OF ENZYME ACTIVITY
1. Allosteric binding sites: Allosteric enzymes are
regulated by molecules called effectors
(modifiers) that binds nonconvalently at a site
other than the active site.
2. By Covalent Modification: Many enzymes are
regulated by covalent modification, most
frequently by the addition or removal of
phosphate group to serine, threonine or
tyrosine residue of the enzyme by kinases.
(enzyme)
3. Induction and repression of enzyme
sysnthesis: Cells can also regulate the amount of
enzymes present by altering the rate of enzyme
synthesis.
REGULATION CONT.
4. Zymogen Cleavage: Some enzyme are
synthesized as inactive precursor, called
zymogens, that are activated by proteolysis (e.g.,
digestive enzyme, pepsinogen is inactive and
cleaved to pepsin which is active chymotrypsin)
5.Location within the cell: Many enzymes are
localized in specific organelles within the cell.
This, compartmentation helps in the regulation of
the metabolic pathway.
9. Enzymes in clinical diagnosis
An enzyme test is a blood test or urine test that
measures levels of certain enzymes to assess how well
the bodys systems are functioning and whether there
has been any tissue damage. (why?)
Principal Serum Enzymes Used in Clinical Diagnosis.
Note: Many of the enzymes are not specific for the disease listed.
Some diseases caused by enzyme malfunctions
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Thank You