Using lysozyme as an example, what can an enzyme’s structure reveal about its catalytic mechanism?

What is meant by substrates of enzymatic reactions?

How temperature, pH and salt affects the enzyme activity in terms of protein structure (primary, secondary, tertiary, quaternary) and other factors? Please explain briefly.

Please answer this question and the highlighted question is wrong please explain why and give me the correct answer

Describe the specific multi-enzyme example discussed in class of how enzyme activity can be altered by changing its substrate to product ratio.

Discuss in a short paragraph (3–5 sentences for each mutation) whether or not the enzyme is likely to completely lose catalytic activity if the following mutations are carried out. You may assume that steric effects do not distort the active site so much that catalysis cannot take place; focus your analysis on discussing the chemistry the amino acid side chains are able to perform and the properties that enable them to do so.   Mutation 1: H to E Mutation 2: H to N Mutation 3: S to D Mutation 4: S to C

Using the Acronym LILHOT, give the 6 major families of enzymes found in biological systems

Inhibitors are compounds capable of blocking the catalytic process. Outline with the use of graphs and equations in illustrating the different modes of action of enzyme inhibitors.

Find an enzyme that is used by humans for some industrial or useful process (apart from its original purpose; e.g. food production, textiles, agriculture, clinical diagnosis, medical treatment, biofuel production, material polymerization, etc.).   How do we obtain or harvest the enzyme?   What reaction(s) does it catalyze, and how is this useful for its industrial purpose?   200 words only

Can you explain the following based on its mode of enzyme kinetics:  1) Synthesis/degradation of enzymes 2) Allosteric regulation  3) Covalent modification