# 5 Page 2 of 3 Question 4. Consider the enzyme alkaline phosphatase from E. col

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Page 2 of 3 Question 4. Consider the enzyme alkaline phosphatase from E. coli. a. What is its EC number? 3 b. What is its quaternary structure (name and nomenclature)? c. What cofactor(s) does it require for activity? Question 5. Consider the protease trypsin. a. What is its normal catalytic activity? b. Can it catalyze the formation of peptide bonds? Why or why not? c. Does it do so normally in the body? Why or why not? 1 estion 6. Here is a list of experiments you might do to determine the mechanism of action of newly purified enzymes and potential results. each result indicates about the enzymes' mechanisms. Be explicit wh appropriate (ie WHICH amino acid(s) might be involved and what min Note: treat each result independentl no pronertionl

Explanation / Answer

Trypsin is a medium size globular protein that functions as a pancreatic serine protease

This enzyme hydrolyzes bonds by cleaving peptides on the C-terminal side of the amino acid residues lysine and arginine. It has also been shown that cleavage will not occur if there is a proline residue on the carboxyl side of the cleavage site. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline.

It does so normally in the body. A peptide bond is a chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, releasing a molecule of water (H2O). This is a dehydration synthesis reaction (also known as a condensation reaction), and usually occurs between amino acids. So it is normally possible. But Im not very sure on this answer, please confirm this once again.

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