ChemistryBrief Explanation. 

Define the specific catalytic mechanisms below:

a. General acid-base catalysis

b. Covalent catalysis

c. Metal ion catalysis

d. Electrostatic catalysis

Briefly explain the mechanism of chymotrypsin, specifically mentioning the role of its amino acids Ser195, His57, Asp102, andGly193. Also, describe the role of the hydrophobic pocket and oxyanion hole.

What role do cofactors, such as the two magnesium in enolase play in many enzymes?

When must enzyme kinetics be performed in a reaction (early or late) and why?

Hexokinase interacts with substrates such as ATP(Km = 0.4 mM) and glucose (Km = 50 M). Which of the two substrates has a higher affinity? Should Km always be used as an indicator of affinity?