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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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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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