A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere with substrate binding or catalysis are inhibitors. Identify the type of inhibition associated with each of the descriptions and examples by classifying each statement as irreversible, competitive, or mixed inhibition.
Enzyme kinetics
In biochemistry, enzymes are proteins that act as biological catalysts. Catalysis is the addition of a catalyst to a chemical reaction to speed up the pace of the reaction. Catalysis can be categorized as either homogeneous or heterogeneous, depending on whether the catalysts are distributed in the same phase as that of the reactants. Enzymes are an essential part of the cell because, without them, many organic processes would slow down and thus will affect the processes that are important for cell survival and sustenance.
Regulation of Enzymes
A substance that acts as a catalyst to regulate the reaction rate in the living organism's metabolic pathways without itself getting altered is an enzyme. Most of the biological reactions and metabolic pathways in the living systems are carried out by enzymes. They are specific for their works and work in particular conditions. It maintains the best possible rate of reaction in the most stable state. The enzymes have distinct properties as they can proceed with the reaction in any direction, their particular binding sites, pH specificity, temperature specificity required in very few amounts.
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A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere with substrate binding or
catalysis are inhibitors. Identify the type of inhibition associated with each of the descriptions and examples by classifying
each statement as irreversible, competitive, or mixed inhibition.
Irreversible inhibition
Competitive inhibition
Mixed inhibition
binding by the inhibitor does not affect Vmax
inhibitor may permanently modify an enzyme
binding by the inhibitor decreases Vmas
the Alt ion binds to acetylcholinesterase or
to the acetylcholinesterase-substrate complex
DIPF permanently modifies the hydroxyl
a transition state analog binds reversibly
to isomerase
group of a Ser residue at the active site
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