ENZYMES

Enzymes

Substances that act as catalysts, increasing the rate of chemical reactions without being consumed.

Pathologic Causes

Elevated enzyme levels due to disease or injury.

Physiologic Causes

Elevated enzyme levels due to normal bodily functions or processes.

Plasma-Specific Enzymes

Enzymes primarily found in plasma or blood.

Non-Plasma-Specific Enzymes

Enzymes present in various tissues, not restricted to blood plasma.

Lactate Dehydrogenase (LDH)

An enzyme involved in energy production, found in many tissues.

Creatine Kinase (CK)

An enzyme involved in energy metabolism, primarily found in muscle and brain.

Biomarkers

Substances used to indicate tissue damage or disease.

Active Site

The region on an enzyme where the substrate binds.

Substrate

The reactant that enzymes act upon during a biochemical reaction.

Product

The result of the enzyme-substrate reaction.

Factors Affecting Enzyme Activity

Temperature, pH, substrate concentration, enzyme concentration, presence of inhibitors or activators, and free energy.

Michaelis-Menten Equation

A mathematical representation of enzyme kinetics, relating reaction velocity to substrate concentration.

Vmax

The maximum rate of reaction for an enzyme.

Km

The substrate concentration at which the reaction rate is half of Vmax.

Turnover Number (kcat)

The number of substrate molecules converted to product per enzyme molecule per second.

Competitive Inhibition

A type of inhibition where the inhibitor competes with the substrate for the active site.

Non-Competitive Inhibition

Inhibition where the inhibitor binds to the enzyme or enzyme-substrate complex, not competing with the substrate.

Uncompetitive Inhibition

Inhibition where the inhibitor binds only to the enzyme-substrate complex.

Allosteric Enzymes

Enzymes regulated by the binding of molecules at sites other than the active site.

Sigmoidal Kinetics

A type of enzyme kinetics characterized by a sigmoidal curve, indicating cooperative binding.

Hyperbolic Kinetics

A type of enzyme kinetics characterized by a hyperbolic curve, typical of non-allosteric enzymes.

Applications of Enzyme Kinetics

Drug design, biotechnology, industrial applications, and clinical diagnostics.

Optimal Temperature

The temperature range at which an enzyme functions best.

Denaturation

The process by which an enzyme loses its functional shape due to extreme conditions.

Optimal pH

The pH level at which an enzyme is most active.

Saturation Point

The point at which increasing substrate concentration no longer increases the reaction rate.

Allosteric Regulation

Regulation of enzyme activity through the binding of effectors at sites other than the active site.

Covalent Modification

A type of enzyme regulation involving the addition or removal of chemical groups.

Industrial Uses of Enzymes

Applications in the food industry, biotechnology, and medical fields.