Enzymes act as biological catalysts that speed up chemical reactions. They do not store genetic information or provide energy directly to cells.

Enzymes are proteins that catalyze biochemical reactions. They are distinct from carbohydrates, lipids, and nucleic acids, which serve different cellular functions.

The active site is the region of the enzyme where substrates bind and the reaction occurs. It is essential for the enzyme's catalytic function.

Enzymes are predominantly composed of proteins, which are made up of amino acids. They are not primarily composed of carbohydrates, lipids, or nucleic acids.

Enzymes lower activation energy by providing an alternative reaction pathway that requires less energy. They do not raise temperature or consume energy in the process.

The induced fit model describes how the enzyme's active site molds itself around the substrate upon binding. This dynamic adjustment is not represented by the lock and key model.

A competitive inhibitor increases the apparent Km by competing with the substrate for the active site, requiring a higher substrate concentration for effective catalysis. It does not change the Vmax since the inhibition can be overcome by further substrate.

Enzyme activity generally rises with temperature until it reaches an optimum, beyond which the enzyme can denature and its activity drops sharply. This behavior highlights the importance of temperature in maintaining enzyme structure.

Coenzymes are organic molecules that transiently bind to enzymes and assist in catalysis. They are not permanent parts of the enzyme's structure nor do they block activity.

High heat can disrupt the hydrogen bonds and other interactions that maintain an enzyme's structure, leading to denaturation. Neutral pH and sufficient coenzyme levels help maintain the proper enzyme configuration.

Substrate specificity means that an enzyme will only bind to a particular substrate or a group of closely related substrates. This specificity is due to the precise shape and chemical environment of the active site.

Even if an enzyme is present, a low substrate concentration means there are fewer molecules available for the enzyme to act on, reducing the reaction rate. Optimal pH, sufficient enzyme, and proper temperature favor faster reactions.

Vmax is the maximum rate of an enzyme-catalyzed reaction when the enzyme is saturated with substrate. It reflects the catalytic capacity of the enzyme and is independent of substrate concentration once saturation is achieved.

Non-competitive inhibitors bind to an allosteric site rather than the active site, reducing the overall number of active enzyme molecules and thus decreasing Vmax. Since they do not compete with the substrate, the Km remains unchanged.

The enzyme-substrate complex is a temporary state in which the substrate is bound to the enzyme's active site, allowing the reaction to proceed efficiently. This complex is crucial for lowering the activation energy needed for the reaction.

Allosteric inhibitors attach to a site other than the active site, which causes a conformational change that reduces the enzyme's activity. This form of regulation is distinct from competitive inhibition since it does not involve direct competition with the substrate.

Enzyme saturation occurs when every enzyme molecule's active site is occupied by a substrate molecule, limiting the reaction rate to a maximum value (Vmax). Adding more substrate beyond this point does not increase the rate because the available active sites are already fully engaged.

Cofactors are non-protein molecules that bind to enzymes and help to stabilize the structure or properly orient substrates within the active site. This assistance increases the enzyme's catalytic efficiency without altering its specificity.

A lower Km value indicates that an enzyme can achieve half-maximum velocity at a lower substrate concentration, which signifies a higher affinity between the enzyme and its substrate. This change does not inherently affect the maximum reaction rate (Vmax).

Michaelis-Menten kinetics analysis is the standard method for determining key parameters such as Km and Vmax of an enzyme. Other techniques like Western blot, X-ray crystallography, and PCR are used for protein identification, structural analysis, and DNA amplification respectively.