Energy and Enzymes (copy)

chemical/potential energy

chemical/potential energy

The energy stored in an object due to its position or composition, which can be released to do work.

kinetic energy

Energy of motion.

metabolism

The process by which the body converts food and drinks into energy, and uses that energy to support various functions and activities.

metabolic/enzymatic pathways

The series of chemical reactions that occur in living organisms to convert molecules into energy or build new molecules. Enzymes, proteins that catalyze these reactions, play a crucial role. They regulate and speed up the reactions, ensuring efficient energy production and molecule synthesis.

catabolism

Process of breaking down complex molecules into simpler ones to release energy.

anabolism

The process in which complex molecules are built from simpler ones, requiring energy input.

closed system

A system that does not exchange matter or energy with its surroundings. It is isolated and operates independently, without any external influences.

entropy

Measure of disorder or randomness in a system. It increases with the number of possible arrangements. It cannot decrease in an isolated system.

open systems

Systems that interact with their environment, allowing the exchange of information, energy, and matter. They are influenced by external factors and can adapt and evolve.

(Gibbs) free energy

Measure of a system's ability to do work at constant temperature and pressure. Determines the spontaneity of a process.

exergonic

Process that releases energy as it occurs, often through the breakdown of complex molecules into simpler ones.

endergonic

Energy-requiring chemical reaction that absorbs energy from its surroundings.

catalytic assistance

A process where a substance helps speed up a chemical reaction without being consumed in the process.

substrates

The molecules on which enzymes act to catalyze a chemical reaction. They bind to the active site of the enzyme and are transformed into products.

Tertiary Structure

The three-dimensional arrangement of a protein's secondary structure elements, resulting from interactions between amino acid side chains. It determines the overall shape and functional properties of a protein.

active site

The region of an enzyme where a substrate binds and undergoes a chemical reaction. It is typically a small and specific area within the enzyme's structure.

adenosine tri-phosphate

Energy molecule used by cells for various metabolic processes. Consists of adenine, ribose sugar, and three phosphate groups. Releases energy when the bond between the last two phosphate groups is broken, forming adenosine diphosphate (ADP) and inorganic phosphate (Pi).

coupling of reactions

The linking of two or more chemical reactions to occur simultaneously, with the product of one reaction becoming the reactant of another.

Saturation (of enzymes)

A state in which all available enzyme active sites are occupied by substrate molecules.

affinity

A strong attraction or liking towards something or someone based on shared qualities, interests, or characteristics. At which the velocity of the reaction is at maximum (Vmax )

factors that effect the rate of enzyme productivity

temperature, pH, substrate concentration, enzyme concentration, presence of inhibitors or activators.

cofactors

Molecules or ions that help enzymes function properly by binding to them. They can be inorganic (like metals) or organic (like vitamins).

Quaternary Structure

The arrangement of multiple protein subunits into a functional, higher-order structure. It refers to the spatial arrangement and interactions between different protein subunits, forming a complex. Enhances protein stability and functionality, allowing for diverse biological functions.

inhibitors

Substances that bind to enzymes or receptors, reducing their activity. They can be competitive, binding to the active site, or non-competitive, binding elsewhere.

Competitive Inhibitor

A substance that competes with the substrate for the active site of an enzyme, blocking its activity. It binds reversibly to the active site, preventing the substrate from binding and inhibiting the enzyme's function. Can be overcome by increasing the concentration of the substrate.

non-competitive inhibition

Type of enzyme inhibition where the inhibitor binds to the enzyme at a different site than the active site, preventing substrate binding and slowing down the reaction rate.

allosteric site

A specific region on an enzyme where molecules other than the substrate can bind, causing a change in the enzyme's activity. This binding can either enhance or inhibit the enzyme's function, regulating its activity.

Allosteric Regulation

A type of enzyme regulation where the binding of a molecule to a specific site, known as the allosteric site, can either enhance or inhibit the enzyme's activity. This regulation occurs through a conformational change in the enzyme's structure, affecting its catalytic function.

Feedback Inhibition

Regulatory mechanism in which the end product of a biochemical pathway inhibits its own production by binding to an enzyme or regulatory protein. This helps maintain homeostasis and prevents excessive accumulation of the end product.