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Enzyme II

The document provides an overview of enzyme kinetics, focusing on the Michaelis-Menten equation, which describes the relationship between reaction velocity and substrate concentration. It discusses key concepts such as Km (Michaelis constant) and Vmax (maximum velocity), as well as different types of enzyme inhibition (competitive, noncompetitive, and uncompetitive) and regulation mechanisms (allosteric regulation, covalent modification, and feedback inhibition). Understanding these principles is essential for studying enzyme activity and metabolic processes.

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0% found this document useful (0 votes)
11 views15 pages

Enzyme II

The document provides an overview of enzyme kinetics, focusing on the Michaelis-Menten equation, which describes the relationship between reaction velocity and substrate concentration. It discusses key concepts such as Km (Michaelis constant) and Vmax (maximum velocity), as well as different types of enzyme inhibition (competitive, noncompetitive, and uncompetitive) and regulation mechanisms (allosteric regulation, covalent modification, and feedback inhibition). Understanding these principles is essential for studying enzyme activity and metabolic processes.

Uploaded by

luci99334455
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PPTX, PDF, TXT or read online on Scribd
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Enzymes

Generic BNS Biochemistry (2nd Semester)


ENZYME KINETICS
The study of enzyme reaction rates is
known as kinetics
Michaelis-Menten Equation
The Michaelis–Menten equation describes how reaction
velocity changes with substrate concentration:
V 0 = initial reaction velocity (is the
rate of reaction as soon as enzyme
and substrates are mixed)
V max = maximum velocity (is
reached when all active sites on the
enzyme are filled with substrate, i.e.
enzyme is in the E-S complex.
K m = Michaelis-Menten constant [is
the substrate concentration, at which
the reaction rate is half of its
maximum velocity (Vmax)].
Assumptions according to the Michaelis–
Menten rate equation.

• At the start of reaction, rate of reaction depends upon


substrate concentration
• The concentration of the ES complex does not change with
time (the steady-state assumption), that is, the rate of
formation of ES is equal to that of the breakdown of ES (to E
+ S and to E + P)
• Initial reaction velocities (vo) are used in the analysis of
enzyme reactions
Significance of Km (Michaelis
Constant)
Km characteristics
 Km is numerically equal to the
substrate concentration at which
the reaction velocity is equal to
one half Vmax
 Km does not vary with enzyme
concentration
 Km, the Michaelis constant, is
characteristic of an enzyme and its
particular substrate and reflects the
affinity of the enzyme for that substrate
Cont.…

a.Small Km: Low Km reflects a high


affinity of the enzyme for
substrate, because a low
concentration of substrate is
needed to half-saturate the enzyme
b.Large Km: High Km reflects a low
affinity of enzyme for substrate
because a high concentration of
substrate is needed to half
saturate the enzyme
Significance of Vmax (Maximal Velocity)

• The rate of the reaction is directly proportional to the


enzyme concentration
• The Vmax of a reaction is an index of the catalytic
efficiency of an enzyme.
• Vmax is reached when all active sites on the enzyme are
filled with substrate, i.e. enzyme is in the E-S complex
ENZYME INHIBITION

• Any substance that can decrease the velocity of an enzyme-


catalyzed reaction is considered to be an inhibitor.
• Inhibitors can be reversible or irreversible
• Irreversible inhibitors bind to enzymes through covalent
bonds
• Reversible inhibitors bind to enzymes through noncovalent
bonds forming an enzyme-inhibitor complex
1. Competitive inhibition
2. Non-competitive inhibition
3. Uncompetitive inhibition
Competitive inhibition

 inhibitor binds reversibly to


the same site that the substrate
would normally occupy and,
therefore, competes with the
substrate for binding to the
enzyme active site
 Vmax remains unchanged
 Km is high
 Statin drugs as examples of
competitive inhibitor
Noncompetitive inhibition
 Noncompetitive inhibition occurs when the
inhibitor and substrate bind at different
sites on the enzyme. The noncompetitive
inhibitor can bind either free enzyme or the
ES complex, thereby preventing the
reaction from occurring
 Vmax is low
 Km remains unchanged
Uncompetitive inhibition

 Uncompetitive inhibitor can bind


only to the enzyme substrate
(ES) complex
 Low V max
 Low Km
ENZYME REGULATION

• The regulation (activation/inactivation of enzyme


activity) of the reaction velocity of enzymes is essential
if an organism is to coordinate its numerous metabolic
processes
• Allosteric regulation
• Covalent regulation
• Feed back inhibition
Allosteric enzymes
• Allosteric enzymes do not follow Michaelis–Menten kinetics but are
regulated by molecules called effectors that bind to them
noncovalently at a site other than the active site.
• Effectors that inhibit enzyme activity are termed negative
effectors,
• Effctors that increase enzyme activity are called positive effectors
• Note: allosteric enzymes frequently catalyze the
committed/rate-limiting step
1. Homotropic effectors : When the substrate itself serves as an
effector, the effect is said to be homotropic
2. Heterotropic effectors: When the effector is a different molecule
than the substrate, it is said to be heterotropic
Covalent modification/Regulation

• Many enzymes are regulated (activated/inactivated) by


covalent modification, by
• Phosphorylation: Kinases causes phosphorylation
• De-phosphorylation: Phosphatases causes
dephosphorylation
Feed back Inhibition

• In multienzyme systems, the first enzyme is inhibited by


the end product
• Whenever the end product of such metabolic reaction
produced in excess of the cell’s needs. The end product of
the pathway acts as a specific inhibitor of the first or
regulatory enzyme in the pathway
• This type of regulation is called feedback inhibition

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