A biochemist is trying to determine the type of proteases they have isolated from walrus blubber. The three proteases and their relative activities in the presence of the indicated non-specific irreversible inhibitors are shown in the table below: Protease a Protease B Protease y Given this data, please answer the following question: The catalytic site of Protease ß contains an important: C R Он + lodoacetate Normal Activity Normal Activity No Activity D + Tetranitromethane Normal Activity No Activity Normal Activity

Compounds I, II, and III are in the following biochemical pathway: precursor compound I enzyme A enzyme B compound II ► compound III enzyme Mutation a inactivates enzyme A, mutation b inactivates enzyme B, and mutation c inactivates enzyme C. Mutants, each having one of these defects, were tested on minimal medium to which compound I, II, or III was added. Fill in the results expected of these tests by placing a plus sign (+) for growth or a minus sign (-) for no growth in the table below. Minimal medium to which is added Strain with mutation Compound I Compound II Compound III

The objective is to study a novel protease P isolated from the digestive tract of an Amazonian insect. This protease can exist into two forms Pi and Pa which have identical amino acid sequences (both of 80 kDa). However, only Pa shows proteolytic activity. To better understand the activation mode of Pi (inactive form) in Pa (active form), the following experiment was done using DIPF. DIPF (diisopropylphosphofluoridate) is a well-known irreversible inhibitor of serine proteases. It reacts with the catalytic serine residue of the active site of proteases as shown below: Enzyme -CH₂OH + CH(CH3)2 O F-P=0 O CH(CH3)2 Diisopropylphospho- fluoridate (DIPF) Enzyme -CH,—O CH(CH3)2 O <=0 O CH(CH3)2 DIP-Enzyme Both proteases Pa and P₁ were incubated with 32P-DIPF for 30 min at 37°C, and then dialysed to remove excess of unreacted radiolabelled reagent. The two proteases were then analyzed in Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE), with and without 2-mercaptoethanol.…

The following data describe the catalysis of cleavage of peptide bonds in small peptides by a protease: Substrate K (1/s) K₁, (mM) k./K₁ (mM/s) A 0.1 10 B 1 1 10 0.1 100 0.02 8,000 0.05 10,000 0.5 Use this information to answer the next three questions. BODEF с D E F 0.01 1 100 5,000 160,000 20,000 4. Which substrate binds to the enzyme with the highest affinity? a. A b. B C. C d. D e. E f. F

Describe type I, II, and III L-asparaginases. Mention characteristics and differences between them with respect to enzyme kinetics (rate, km, etc).

If thymine nucleotides are degraded by the same enzymes as those catabolizing uridine nucleotides, give the structure of the thymine metabolite that corresponds to B-ureidopropionate.

Mechanistic probes often require the use of an electrophilic functional group to interact with an especially-reactive amino acid in the protein active site. For each of the follow functional groups that can be used in a mechanistic probe, provide a structure of the product.    asap

When performing his experiments on protein refolding, Christian Anfinsen obtained a quite different result when reduced ribonuclease was reoxidized while it was still in 8 M urea and the preparation was then dialyzed to remove the urea. Ribonuclease reoxidized in this way had only 1% of the enzymatic activity of the native protein. Why were the outcomes so different when reduced ribonuclease was reoxidized in the presence and absence of urea?

Draw the structure of the PTH derivative product you would obtain by Edman degradation of the following peptides: (a) I-L-P-F   (b) D-T-S-G-A

Please provide Typed solution in details, you can use only handwritten diagram