
How are enzymes able to accomplish such effective catalysis?
Answer
552.3k+ views
Hint: Proteins that function as biological catalysts are enzymes or biocatalysts. Chemical reactions are accelerated by catalysts. The molecules that enzymes can work on are called substrates, and the enzyme transforms the substrates into multiple products known as molecules.
Complete answer:
All the enzymes were once considered proteins, but since the 1980s, it has been shown that the catalytic power of certain nucleic acids, called ribozymes (or catalytic RNAs), undermines this axiom. Although RNA's enzymatic functioning is still very little known, this debate will focus primarily on protein enzymes. Certain enzymes are bound by an external chemical component called a cofactor, which is a direct participant in the catalytic event and thus is essential for enzymatic activity. A cofactor may be either a coenzyme, a vitamin-like organic compound, or an inorganic metal ion; certain enzymes require both.
The enzymes react with the substrate to create an intermediate complex that needs less energy for the reaction to start, a "transition state." In order to form reaction products, the unstable intermediate compound easily breaks down, and the unaffected enzyme is free to react with other molecules of the substrate. A groove or pocket formed by the protein's folding pattern is the active site. Along with the chemical and electrical properties of the amino acids and cofactors within the active site, this three-dimensional arrangement allows only a particular substrate to bind to the site, thus defining the specificity of the enzyme.
A cofactor can be bound to the enzyme either closely or loosely. The cofactor is referred to as a prosthetic community if closely connected. Just a certain region of the enzyme binds to the substrate, called the active site.
Note: 1000 substrate molecules can be transformed per second by a normal enzyme molecule. With increased substrate concentration, the rate of an enzymatic reaction increases, achieving full velocity as all the enzyme molecules' active sites are engaged.
Complete answer:
All the enzymes were once considered proteins, but since the 1980s, it has been shown that the catalytic power of certain nucleic acids, called ribozymes (or catalytic RNAs), undermines this axiom. Although RNA's enzymatic functioning is still very little known, this debate will focus primarily on protein enzymes. Certain enzymes are bound by an external chemical component called a cofactor, which is a direct participant in the catalytic event and thus is essential for enzymatic activity. A cofactor may be either a coenzyme, a vitamin-like organic compound, or an inorganic metal ion; certain enzymes require both.
The enzymes react with the substrate to create an intermediate complex that needs less energy for the reaction to start, a "transition state." In order to form reaction products, the unstable intermediate compound easily breaks down, and the unaffected enzyme is free to react with other molecules of the substrate. A groove or pocket formed by the protein's folding pattern is the active site. Along with the chemical and electrical properties of the amino acids and cofactors within the active site, this three-dimensional arrangement allows only a particular substrate to bind to the site, thus defining the specificity of the enzyme.
A cofactor can be bound to the enzyme either closely or loosely. The cofactor is referred to as a prosthetic community if closely connected. Just a certain region of the enzyme binds to the substrate, called the active site.
Note: 1000 substrate molecules can be transformed per second by a normal enzyme molecule. With increased substrate concentration, the rate of an enzymatic reaction increases, achieving full velocity as all the enzyme molecules' active sites are engaged.
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