There are several factors that regulate enzymes, including genetic regulation, compartmentalization, substrate concentration, degradation of enzymes, environmental factors, modification of zymogens, covalent modification, allosteric regulation, and inhibition. Allosteric proteins show cooperativity where the activity at one site affects others, and their kinetics do not follow the Michaelis-Menten equation. Cooperativity can be positive, facilitating binding at other sites, or negative, inhibiting other sites. Regulatory enzymes can be homotropic, using the same modulator and substrate, or heterotropic, using different modulators and substrates. Isoenzymes are enzymes that catalyze the same reaction but differ in amino acid sequence, while z
There are several factors that regulate enzymes, including genetic regulation, compartmentalization, substrate concentration, degradation of enzymes, environmental factors, modification of zymogens, covalent modification, allosteric regulation, and inhibition. Allosteric proteins show cooperativity where the activity at one site affects others, and their kinetics do not follow the Michaelis-Menten equation. Cooperativity can be positive, facilitating binding at other sites, or negative, inhibiting other sites. Regulatory enzymes can be homotropic, using the same modulator and substrate, or heterotropic, using different modulators and substrates. Isoenzymes are enzymes that catalyze the same reaction but differ in amino acid sequence, while z
There are several factors that regulate enzymes, including genetic regulation, compartmentalization, substrate concentration, degradation of enzymes, environmental factors, modification of zymogens, covalent modification, allosteric regulation, and inhibition. Allosteric proteins show cooperativity where the activity at one site affects others, and their kinetics do not follow the Michaelis-Menten equation. Cooperativity can be positive, facilitating binding at other sites, or negative, inhibiting other sites. Regulatory enzymes can be homotropic, using the same modulator and substrate, or heterotropic, using different modulators and substrates. Isoenzymes are enzymes that catalyze the same reaction but differ in amino acid sequence, while z
biological catalysts, meaning that they help speed up chemical reactions in organisms' bodies. This process is achieved by the binding of enzymes to substrates, the complex molecules that enter cells and upon which enzymes act. Types of Enzyme Regulation
There are certain factors that help regulate enzymes that
include genetic enzyme regulation, compartmentalization, substrate concentration, degradation of enzymes, alteration of environmental factors, modification of zymogens, covalent modification, allosteric regulation, and inhibition. Ty p e s o f E n z y m e R e g u l a t i o n
•Genetic Regulation •Compartmentalization •Substrate •Degradation of
Concentration Enzymes Ty p e s o f E n z y m e R e g u l a t i o n
•Alteration of •Modification of •Covalent •Allosteric
cooperativity i.e., activity at one functional site affects the activity at others. A slight change in substrate concentration can produce substantial changes in activity. Their kinetics do not obey the Michaelis-Menten equation. Their V versus [S] plots yield sigmoid curves rather than hyperbolas. bochins.paw
•Positive cooperativity: Ligand
binding at one site facilitates the binding of other sites on the same molecule. •Negative cooperativity: Ligand binding at one site inhibits the binding of other sites on the same molecule. bochins.paw
Regulatory enzymes for which
substrate and modulators are identical are called Homotropic. When the modulator is a molecule other than the substrate, the enzyme is said to be Heterotopic. Isoenzymes are enzymes that differ in bochins.paw
amino acid sequence yet catalyze the
same reaction. Zymogens are inactive precursors of enzymes. Zymogens or proenzymes acquire full activity only upon specific proteolytic cleavage of one or several of their peptide bond. Irreversible process. bochins.paw