Q19 QUESTION 19Use the following information to answer which enzyme (i.e. Enzyme 1, Enzyme 2 or Enzyme 3) describes each of Questions 1, 2, and 3 (Hint 1:The same enzyme may be the correct response for more than 1 question. Hint 2: Watch your unitsEnzyme 1Enzyme 2Enzyme 3kcat5x 103 S-126 x 105-140 x 10 4 -1keatCatalyticefficiency KmKM90 x 10-4 M-310 mx 10 M8 x 10-6 MWhich enzymne has the highest affinity for the substrate?A. Enzyme 2Which enzyme converts the most substrate to product in a give time B. Enzyme 3period?C. Enzyme 1+ Whihc Enzyme has the highest catalytic efficiency?

The Michaelis Menten constant (KM) can be used to define the affinity of an enzyme towards its…

Answered: Which enzymne has the highest affinity…

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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QUESTION 1 Enzyme concentration affects the rate of an enzymatic reaction by It actually has no effect on the reaction rate. by increasing the rate of reaction when it is low. by decreasing the rate of reaction when it is high by increasing the rate of reaction when it is high. Click Save and Submit to save and submit. Click Save All Answers to save all answers. OCT 16 000 F3 000 F4 F5 F6 F7 F8
Question 8 Match the microbial function(s) with the most appropriate nutrient type. Support enzymatic activity in the cell, in relatively high concentrations 10 Required at relatively low concentrations to support certain enzyme functions Act as organic co-enzymes or functional groups of enzymes Components needed in relatively high amounts in cytochromes and electron carrier proteins in respiration Required as precursors for nucleic acid biosynthesis Required in relatively high concentrations for protein translation < Previous [Choose ] [Choose ] Micronutrients Cofactor macronutrients Vitamin growth factors Purine or pyrimidine growth factors Amino acid growth factors [Choose ] [Choose ] [Choose ] [Choose ]
QUESTION 14 Choose the order of reactions that best describes a metabolic pathway catalyzed by enzymes First the substrate binds an active site, 2-induced fit occurs, 3-enzyme is degraded and product released First the Enzyme binds its substrate, 2- Substrate is converted to product, 3- Enzyme is reused First the Enzyme binds its substrate, 2-Substrate is converted to product, 3-Enzyme is degraded First the active site binds a substrate, 2-Active site changes to product, 3- Enzyme changes shape
Question 4 Temoporfin (Foscan) is a photosensitizer used in photodynamic therapy for the treatment of squamous cell carcinoma of the head and neck. The prodrug is not being activated by internal enzymes but activated by light as an external stimulus. What is the benefit of this design? O To achieve spatiotemporal control of the killing of cancer cells. O More bioorthogonal as it does not introduce addition chemicals into the body. O To only target superficial cancer cells within the penetration depth of light. O More convenient for patients as they can activate foscan by staying in the sun.
QUESTION 9 Cyanogen bromide cleavage of a peptide results in 3 fragments with the sequence: AGRFM, RS, and AKEM. Proteolysis with trypsin results in the fragments: S, FMAK, EMR, and AGR. The sequence of the peptide is [A]. CS Scanned with CamScanner
Question 15 The following molecules are separated using size exclusion chromatography. Give an order in which they elute from the column (which come first, second..). a. Myoglobin (17 kDa) and amylase (55 kDa) b. Vitamin B12 (1.5 kDa) and albumin (67 kDa) c. Cytochrome C (12 kDa) and ribonuclease A (13 kDa)
Question 18 One of the termination mechanisms in bacteria utilizes the factor that is an ATP-dependent helicase. (answer in words and not in Greek symbol) Blank 1 Blank 1 Add your answer
QUESTION 1 You have a crude lysate sample (CL) containing a mixture of six proteins (1, 2, 3, 4, 5, ẞ- galactosidase), and your goal is to obtain purified ẞ-gal. Some characteristics of these proteins are shown in the table below. Protein Alcohol dehydrogenase Carbonic anhydrase Insulin B chain Phosphorylase B Glutamic dehydrogenase B-galactosidase Concentration of ammonium sulfate (AS) required for precipitation Molecular Weight (kDa) Isoelectric point (pl) 45% 38 3.7 80% 65% 20% 30% 45% 28 4.8 4 5.3 98 68 49 9.5 115 5.3 You begin your purification by performing an ammonium sulfate (AS) precipitation. You add the appropriate concentration of AS to your CL sample, incubate overnight at 4°C, then centrifuge to generate a supernatant (AS-S) and pellet (AS-P). What concentration of AS will you use to precipitate ẞ-galactosidase? O 20% O 30% O 45% 65% O 80%
QUESTION 45 Muscular dystrophy is a disease condition that can be linked to the malfunctioning of proteasomes. O True O False
Question 18 Ser iesi Se les2 Linear (Seriesd) Linear (Series2) 120 100 80 60 40 20 10 12 -20 what type of inhibition is shown and where does the inhibitor bind to the enzyme? non competitive and active site noncompetitive and active site Ocompetitive and active site competitive and inhibitory site
QUESTION 10 Name the structure(s) labeled with the X. 400x
Question 12 (1 point) Listen You are working in the lab with Streptococcus pyogenes and two other bacteria. You streak all three of these microbes onto a Blood Agar plate and observe the following: All of the bacteria grow on the plate but there is a large zone of clearing around S. pyogenes, and no zone of clearing on the other two bacteria. Based on these results what type of Medium is Blood Agar? O A) Blood agar is a culture medium. B) Blood Agar is a selective medium. C) Blood agar is a differential medium. O D) Blood agar is an exclusion medium. O E) Blood agar is a counting medium. 98% 99+

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Which enzymne has the highest affinity for the substrate? A. Enzyme 2 Which enzyme converts the most substrate to product in a give time B. Enzyme 3 period? C. Enzyme 1 Whihc Enzyme has the highest catalytic efficiency?