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-specificirreversible inhibitors are shown in the table below:Protease aProtease BProtease yGiven this data, please answer the following question:The catalytic site of Protease y contains an important:сHY+ lodoacetateNormal ActivityNormal ActivityNo ActivityR+ TetranitromethaneNormal ActivityNo ActivityNormal Activity

The modification of amino acid side chains using amino acid specific covalent labeling is an…

Answered: A biochemist is trying to determine the…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Which of the following statements is not true about the catalytic triad in chymotrypsin? Group of answer choices the side chain of the serine 195 is hydrogen bonded to the imidazole ring of histidine the -NH group of the imidazole ring of histidine is hydrogen bonded to the carboxylate group of aspartate 102 the histidine residue serves to position the aspartate 102 side chain and to polarize its carboxylate group so that it is poised for deprotonation histidine acts as a general base catalyst none of these
During the early stages of an enzyme purification protocol, when cells have been lysed but cytosolic components have not been separated, the reaction velocity-versus-substrate concentration is sigmoidal. As you continue to purify the enzyme, the curve shifts to the right. Explain your results. This is an allosteric enzyme and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly. This is an enzyme that displays Michaelis-Menten kinetics and you purify away an inhibitor. This is an allosteric enzyme and during purification you purify away an activator. This is an allosteric enzyme displaying a double-displacement mechanism and during purification you purify away one of the substrates: This is an enzyme that displays Michaelis-Menten kinetics, and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly.
Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions:(a). How do I determine the enzyme activity? Please give the unit. (b) How do I get the specific activity of this enzyme? Please give the unit.
BIM-46187 is a protein inhibitor that binds to the a-subunit of the G. protein. It prevents the GDP/GTP exchange and prevents activity of the G protein. Which of the following would you expect to see lower levels of as a result? You can select more than or answer. S-S NH2 Mol. M: 795.11 Image: https://aobious.com/aobious/protein-inhibitors/1086-bim-46187.html Select one or more: O a. Cyclic AMP (CAMP) O b. Tyrosine kinase O . HSP O d. Adenylyl Cyclase (AC) O e. DAG O f. JAK O g. IP3
What is the importance in glycosylation in rtPA in terms of its activity as a protein therapeutic?
Describe a common feature at the active site of serine proteases and acetyl cholinesterase
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).
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?
Please provide Typed solution in details, you can use only handwritten diagram

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