Biochemistry Enzymes and Coenzymes Quiz

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Enzymes accelerate chemical reactions without being consumed in the process. They are like biological catalysts, speeding up biochemical reactions within living organisms.

Most enzymes are made up of proteins. They can exist individually, referred to as simple enzymes, or as a complete unit called a holoenzyme. Holoenzymes consist of a protein part called an apoenzyme and a non-protein component called a cofactor. Coenzymes are organic molecules that are loosely attached to the enzyme and aid in its function.

They are produced inside cells but release their activity outside the cells. For example, digestive enzymes like pepsin and α-amylase are produced in the stomach and small intestine, respectively, but exert their action on food in the digestive tract.

They are synthesized and perform their function within the cells. For example, metabolic enzymes like ALT and AST play crucial roles in cellular metabolism.

The substance that the enzyme acts upon. It's like the ingredient that the enzyme modifies to create a product.

They are produced and function within the cell. Some are synthesized in the cytoplasm, while others are made in the endoplasmic reticulum. A small number of enzymes are synthesized in the mitochondria. These enzymes are essential for various cellular processes.

Enzymes are present in all body cells, both in the extracellular fluids like plasma and cerebrospinal fluid (CSF) and within the intracellular compartments of cells. They participate in a wide range of biochemical reactions crucial for life.

The international unit (IU) defines the amount of enzyme required to convert 1 micromole of substrate into product per minute. One unit is equivalent to one micromole per minute. This is a standard measure used to quantify enzyme activity.

A coenzyme involved in transferring acyl groups of fatty acids, activating them for metabolism, and participating in oxidative decarboxylation.

A coenzyme essential for transamination, decarboxylation, and desulfuration of amino acids, playing a crucial role in amino acid metabolism.

A coenzyme involved in the oxidative decarboxylation of pyruvate and α-ketoglutarate, crucial for energy production.

A small molecule that carries hydrogen atoms and electrons, playing a critical role in cellular respiration.

A coenzyme that is essential for the fixation of carbon dioxide, a critical step in photosynthesis and other metabolic pathways.

Enzymes that require a metal ion for activity, but the metal is not tightly bound and can be removed by dialysis.

Enzymes that require a metal ion tightly bound for their function, which cannot be removed by dialysis..

The metal ion in a metalloenzyme is vital for its three-dimensional structure, maintaining its shape for proper function.

Metal ions in metalloenzymes can directly interact with substrate molecules, facilitating their binding to the enzyme.

Some metal ions in metalloenzymes contribute to the formation of a bridge between the enzyme and a coenzyme, enhancing their collaboration.

The specific region of an enzyme where substrate binding and catalysis occur, containing two distinct sites.

The site within the active site of an enzyme where the substrate molecule binds.

The site within the active site of an enzyme where the chemical reaction is catalyzed.

Refers to the number of substrate molecules transformed into products per unit of time by a single enzyme molecule.

A naming system used to classify enzymes based on their reaction type, functional group, coenzyme, and substrate.

The ability of an enzyme to bind and catalyze reactions with specific molecules, excluding others.

An enzyme that acts on only one substrate, showing a high degree of specificity.

An enzyme that acts on molecules sharing a particular functional group, showing a moderate level of specificity.

Enzymes that accelerate reactions by lowering the activation energy required for the reaction to occur.

The substance upon which an enzyme acts, undergoing a chemical transformation.

Molecules that are transformed by enzymes into products.

These enzymes use hydrogen peroxide (H₂O₂) or organic peroxides as substrates. They are involved in the breakdown of these reactive molecules protecting cells from damage.

They reduce peroxides using various electron acceptors like ascorbate, quinones, and reduced glutathione.

Catalase uses hydrogen peroxide as both an electron donor and an electron acceptor.

They directly transfer and incorporate oxygen into a substrate molecule, leading to modifications within the molecule.

They protect aerobic organisms from the damaging effects of superoxide anion free radical (.O₂⁻), a reactive molecule that can harm cells.

The region on an enzyme where the substrate binds and the chemical reaction occurs.

A site on an enzyme where a molecule different from the substrate binds, often leading to a change in the enzyme's activity.

A molecule that binds to an allosteric site and alters the enzyme's activity.

An effector that increases the enzyme's activity.

An effector that decreases the enzyme's activity.

A type of allosteric regulation where the end product of a metabolic pathway inhibits the activity of an enzyme earlier in the pathway.

Regulation of enzyme activity by controlling the amount of enzyme produced.

The process of adding or removing a phosphate group to an enzyme, which can activate or inactivate it.