biochem module 6

Ergon/o

Work/ Energy

Endergonic

A process that requires energy input.

Trop/o

Turning/ Change

Entropy

A measure of disorder or randomness in a system.

Bol/o

Change/Transformation

Catabolism

The breakdown of complex molecules into simpler ones.

Glyc/o

Sugar

Glycolysis

The metabolic pathway that converts glucose into pyruvate.

Thromb/o

Clot

Thrombosis

The formation of a blood clot inside a blood vessel.

Pulmon/o

Lung

Pulmonologist

A physician specializing in lung conditions.

Embol/o

Blockage/Obstruction

Pulmonary Embolism

A blockage in one of the pulmonary arteries in the lungs.

Cardi/o

Heart

Cardiologist

A doctor specializing in heart conditions.

Spir/o

Breathe

Respiratory

Pertaining to the process of breathing.

Acet/o

Vinegar, Acetic acid

Acetate

A salt or ester of acetic acid.

Pyr/o

Fire

Pyrogens

Biomolecules that trigger fever.

Meta-

After, Beyond, Change

Metabolism

The set of life-sustaining chemical reactions in organisms.

Allo-

Other

Allopathic Medicine

A system of medicine that aims to combat disease by using remedies which produce effects different from those produced by the disease.

Intra-

Within

Intracellular

Located or occurring within a cell.

Extra-

Outside, Beyond

Extracellular

Located or occurring outside a cell.

En-

In, Inside, Within

Encephalitis

Inflammation of the brain.

Exhale

To breathe out.

Exo-

Out, Away from, Outside

Endo-

Within

Anabolic

Relating to the process of building up or synthesizing complex molecules.

Ana-

Up, Back, Again, Throughout

Cata-

Breaking down, Decomposition

-ase

Enzyme

Lactase

An enzyme that breaks down lactose.

-ism

Condition, State, Process

Hyperthyroidism

A condition in which the thyroid gland is overactive.

-lysis

Loosening, Breaking down, Dissolution

-ate

Salt or Ester

Acetate Salts

Salts derived from acetic acid.

-zyme

Ferment/yeast

-ose

Sugar/Carbohydrate

Glucose

A simple sugar that is an important energy source.

Lactose

A sugar found in milk.

-ic

Pertaining to

-y

Condition/ State

Modulator

A process of changing, adjusting or regulating the activity or function of a biological system, molecule or enzyme.

Enzyme

Biological catalyst that speeds up chemical reactions.

Citric acid cycle

A series of chemical reactions used by all aerobic organisms to generate energy.

What are enzymes?

Enzymes are proteins that act as biocatalysts to accelerate chemical reactions.

What is the function of enzymes in chemical reactions?

Enzymes increase reaction rates by lowering the activation energy required for the reaction.

What is the typical naming convention for enzymes?

Enzyme names typically end in -ase.

What is the active site of an enzyme?

The active site is the region of the enzyme that is complementary to the substrate, allowing for binding.

What analogy is used to describe enzyme-substrate interaction?

The Lock and Key analogy: the substrate is the key, and the active site is the lock.

What factors can impact enzyme velocity?

Factors include pH, temperature, concentration of ions, and regulatory factors.

What is the unit of reaction rate (V0) for enzymes?

The unit of reaction rate is concentration per minute, such as mM/min.

What is the relationship between substrate concentration ([S]) and reaction rate (V0)?

The relationship is hyperbolic, meaning as substrate concentration increases, the reaction rate approaches a maximum.

What is the role of Alcohol Dehydrogenase (ADH) in the body?

ADH processes alcohol (ethanol) primarily in the liver, converting it to acetaldehyde and then to acetate.

Why is acetaldehyde significant in alcohol metabolism?

Acetaldehyde is toxic and a known carcinogen, but it is quickly converted to acetate to prevent accumulation.

What is the Michaelis-Menten Equation?

The equation is V0 = (Vmax [S]) / (Km + [S]), describing the hyperbolic kinetics of enzyme reactions.

Who developed the Michaelis-Menten Equation?

The equation was developed by Leonor Michaelis and Maud Menten.

What does Vmax represent in the Michaelis-Menten Equation?

Vmax represents the maximal velocity of the enzyme-catalyzed reaction.

What does Km represent in the Michaelis-Menten Equation?

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

How does enzyme concentration affect reaction rates?

A small number of enzyme copies can significantly increase the reaction rate due to their catalytic efficiency.

What is a biocatalyst?

A biocatalyst is a substance, such as an enzyme, that accelerates a chemical reaction without being consumed in the process.

What is the significance of enzyme regulation?

Enzyme regulation allows cells to adapt to changing conditions and maintain homeostasis.

What happens to reaction rates when activation energy is lowered?

Lowering activation energy increases the probability of the reaction occurring and raises the reaction rate.

What is the importance of understanding enzyme kinetics?

Understanding enzyme kinetics is crucial for recognizing how enzymes function and their clinical relevance in various conditions.

What does Vmax represent in enzyme kinetics?

Maximal velocity of an enzyme-catalyzed reaction.

What is the Michaelis-Menten constant (Km)?

The substrate concentration at which the reaction velocity is half of Vmax, approximately 0.3 mM for alcohol dehydrogenase.

What is the significance of hyperbolas in enzyme kinetics?

They represent the relationship between substrate concentration and reaction velocity, indicating that constants like Vmax and Km are estimated.

What is the Lineweaver-Burke approach?

A method that transforms Michaelis-Menten data into a straight line to more reliably estimate Vmax and Km.

How does a competitive inhibitor affect Vmax and Km?

Vmax remains unchanged while Km increases.

What is the effect of a mixed (noncompetitive) inhibitor on Vmax and Km?

Vmax decreases and Km increases.

What happens to Vmax and Km with an uncompetitive inhibitor?

Both Vmax and Km decrease.

What is feedback inhibition in enzyme regulation?

A regulatory mechanism where the product of a pathway inhibits the first enzyme, preventing overproduction.

What is the role of allosteric enzymes?

They are regulated by modulators that bind at sites other than the active site, affecting enzyme activity.

What is the process of phosphorylation in enzyme regulation?

The addition of a phosphate group to an enzyme, which can change its activity and is reversible.

What is proteolytic cleavage?

A non-reversible covalent regulation where inactive enzyme precursors are activated by the removal of specific amino acid sequences.

What triggers the activation of digestive proteases?

The arrival of food in the digestive tract.

What is the blood clotting cascade?

A series of events leading to the activation of fibrin, forming a blood clot in response to injury.

What is the role of vitamin K in blood clotting?

It acts as a coenzyme for glutamate carboxylase, which is essential for the carboxylation of clotting factors.

How do blood thinners like warfarin work?

They inhibit vitamin K activity, reducing the carboxylation of clotting factors and thus decreasing blood clotting.

What are the physiological situations that activate glycogen breakdown?

Low blood glucose levels trigger glucagon and epinephrine release, activating phosphorylase.

What is the difference between phosphorylase a and b?

Phosphorylase a is active and releases glucose, while phosphorylase b is inactive and does not release glucose.

What is the significance of reversible enzymes in metabolic pathways?

They are rarely regulated and allow for flexibility in metabolic control.

What is the effect of covalent modifications on enzyme activity?

They can either activate or deactivate enzymes, depending on the modification.

What are the common types of enzyme regulation?

Covalent and non-covalent regulation, including allosteric regulation and feedback inhibition.

What is the function of kinases and phosphatases?

Kinases transfer phosphate groups to enzymes, while phosphatases remove them.

How do enzymes in extracellular spaces differ from intracellular enzymes?

Extracellular enzymes often function independently and can be activated quickly when needed.

What is the relationship between enzyme activity and substrate concentration?

Enzyme activity typically increases with substrate concentration until a maximum velocity (Vmax) is reached.

What is an example of a reversible enzyme regulation mechanism?

Phosphorylation and dephosphorylation of enzymes.

What is the role of modulators in allosteric regulation?

They bind to allosteric sites, altering the enzyme's conformation and activity.

What is the significance of enzyme kinetics in laboratory experiments?

It helps determine the efficiency and regulation of enzyme activity under various conditions.

What is the impact of substrate concentration on enzyme-catalyzed reactions?

Higher substrate concentrations can increase reaction rates until saturation is reached.