BIOC 203 Enzymology Course Criteria

The word 'enzyme' is derived from a Greek word meaning 'in yeast,' indicating that these catalysts are present inside cells. In the late 1800s, scientists studied the fermentation of sugars by yeast cells. Vitalists claimed that intact cells were needed for fermentation, while mechanists claimed that enzymes in yeast cells catalyze the reactions of fermentation.

The general properties of biological catalysts include specificity, efficiency, regulation, and sensitivity to environmental factors. These properties are used to classify and name enzymes based on their function and structure.

Factors affecting enzyme activity include temperature, pH, substrate concentration, enzyme concentration, and the presence of inhibitors or activators. These factors can significantly impact the rate of enzymatic reactions and ultimately influence biological processes.

Cofactors, such as coenzymes, play a crucial role in enzyme function by assisting in catalytic reactions. Examples of coenzymes include NAD+, FAD, and coenzyme A, each with distinct chemical structures and specific functions in enzyme-catalyzed reactions.

The Michaelis-Menten equation describes the kinetic behavior of enzymes catalyzing one-substrate reactions. It relates the rate of the reaction to the concentration of the substrate and the enzyme's affinity for the substrate, providing insights into the enzyme's efficiency and reaction velocity.

An enzyme is a biological catalyst that speeds up chemical reactions in living organisms. Enzymes are proteins with distinct features such as specificity, efficiency, and the ability to be regulated, which differentiate them from non-enzymatic catalysts.

The Michaelis-Menten equation describes the rate of enzymatic reactions involving a single substrate. It relates the rate of formation of the product to the concentration of the substrate and the enzyme's affinity for the substrate.

Zymogens are inactive enzyme precursors that are converted into active enzymes by proteolytic cleavage. They play a crucial role in regulating enzyme activity and preventing unwanted or premature activation of enzymes.

Vitalists believed that intact cells were necessary for fermentation, while Mechanists argued that enzymes in yeast cells catalyze the reactions of fermentation. This debate highlighted the significance of enzymes as cellular catalysts and their role in biochemical processes.

Factors affecting enzyme activity include temperature, pH, substrate concentration, enzyme concentration, and the presence of inhibitors or activators. These factors can impact the rate and efficiency of enzymatic reactions.

The allosteric site is a specific site on the enzyme, separate from the active site, where a molecule (allosteric regulator) can bind and affect the enzyme's activity. This binding can either enhance or inhibit the enzyme's function, thereby regulating the enzyme's activity in response to various cellular signals.

Zymogen is an inactive precursor of an enzyme that requires a specific cleavage or modification to become active. An example of its importance in clinical biochemistry is the zymogen prothrombin, which is converted into the active enzyme thrombin during the blood clotting process.

The estimation of isoenzyme enzyme activity involves separating different forms of an enzyme based on their unique properties, such as electrophoretic mobility or substrate specificity. This is typically done using techniques like gel electrophoresis. The activity is measured in units, and the analysis of isoenzyme patterns can provide valuable diagnostic information in clinical biochemistry.

The study of fermentation by yeast cells in the late 1800s was pivotal in the debate between Vitalists and Mechanists regarding the role of enzymes. It demonstrated that enzymes in yeast cells catalyze the reactions of fermentation, challenging the Vitalists' claim that intact cells were needed for fermentation. This led to a shift towards the mechanistic view, emphasizing the role of enzymes as catalysts in biochemical reactions.

Enzyme inhibitors are molecules that can bind to the enzyme and decrease its activity. They can be classified as reversible or irreversible inhibitors. Examples include competitive inhibitors (compete with the substrate for the active site), non-competitive inhibitors (bind to the allosteric site), and uncompetitive inhibitors (bind to the enzyme-substrate complex).