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How is enzyme activity regulated in biological systems?
Enzyme activity in biological systems is regulated through various mechanisms such as allosteric regulation, competitive and non-competitive inhibition, post-translational modifications, and gene regulation. These processes help control the rate of enzyme-catalyzed reactions and ensure that they occur at the right time and in the right amount within the cell.
What is the major cation in the intracellular fluid?
potassium
What influences the function of an enzyme?
Enzymes are special proteins that act as catalysts within the body. Each enzyme has a specifically shaped active site for a specific substrate to "slide" into and react. Enzymes are very sensitive to both pH and temperature; altering one or both will cause an enzyme to "denature" and lose its shape, therefore keeping the substrate from fitting into the active site and ultimately stopping these reactions.
What is role of metal ion in enzyme catalysis?
On each surface of enzyme there are detachable cofactor (non-protein portin of enzyme) called activators. Activators are metal ions.Enzymes are proteins and literally fold into a specific 3d structure, to make space for an active site (also called activators). Active site has a shape that fits with specific substrate molecules.The enzyme and substrate form a temporary enzyme-substrate complex.Enzymes are flexible structures.When enzyme and substrate bind together, the shape of enzyme molecule undergoes slight change.This produces strain in chemical bond in the substrate molecules and as a result these bonds break and bonds are formed. These stresses encourage a link between two substrstes leading to the formation of a different molecule.As the result of the chemicl interactions within the active sites a new chemical compound is formed. The new chemical compound is called product.This product is released from the active site, the enzyme assumes its orignal shape and is free to work again.
What are the two factors that effect the efficiency of an enzyme?
Two factors that affect the efficiency of an enzyme are temperature and pH. Enzymes work best within a specific temperature and pH range, and deviations from these optimal conditions can denature the enzyme leading to decreased efficiency. Additionally, substrate concentration plays a role in enzyme efficiency as higher substrate concentrations can lead to faster reaction rates until all enzyme active sites are saturated.
What does the wrong pH do to the shape of an enzyme?
A wrong pH can affect the shape of an enzyme by disrupting the interactions between the enzyme's amino acid residues, leading to a change in the enzyme's conformation. This can affect the enzyme's active site, making it less effective at catalyzing reactions.
The ability of an enzyme to catalyze a reaction is not affected by?
The ability of an enzyme to catalyze a reaction is not affected by changes in temperature or pH within a certain range known as the enzyme's optimal conditions. However, extreme changes in temperature, pH, or enzyme concentration can denature the enzyme and affect its activity. Additionally, the substrate concentration can affect the rate of reaction up to a point of saturation, where all enzyme active sites are occupied.
Why pH is relevant to an enzyme and function?
QUICK ANSWERLiving organisms depend on a proper balance of hydrogen and hydroxide ions in order to maintain essential physiological processes. Scientists use pH to express the concentration of hydrogen ions in a solution. Many organisms have tightly regulated systems to maintain the pH within the required range.
If an enzyme is exposed to an unfavorable pH?
Enzymes shows different enzyme activity in different pH value.If the pH is high or low than the optimum pH there is a decrease in the activity of the enzyme.But if the pH is very high or very low it may lead to the deactivation of the enzyme.
How does malonate inhibit NADH?
Malonate inhibits NADH by competing with NAD+ for binding to the active site of enzyme NADH dehydrogenase within the electron transport chain. This competition prevents NADH from donating electrons to the enzyme, disrupting the flow of electrons and inhibiting ATP production.
What is an inhibitor that forms a covalent bond with an amino acid side group within the active site?
A covalent inhibitor is one that forms a stable covalent bond with an amino acid residue within the active site of an enzyme. This kind of interaction can irreversibly inhibit the enzyme's activity by blocking its active site or altering its structure. Examples include penicillin binding to serine in the active site of penicillinase.
What happen to an enzyme when it perform its function what does this mean about enzyme molecules?
Nothing. The enzyme is not changed by the process of lowering the activation energy of the reaction with the substrates. In their active site some enzymes just give two substrates a protected area for a reaction, some stress bonds thus causing a reaction and some preform catabolically within their active site using their R groups. Regardless of the enzymes activity it is not changed and goes on to perform many processes in the cell.
