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

Cell biology is considered as the study of cells, their structure, and their functions. The cells…

Answered: Compounds I, II, and III are in the…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 25P: Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the...

See similar textbooks

Similar questions

A purified protease enzyme from the fungus Aspergillus sp. Is tested in a laboratory. This enzyme was lyophilized as a white powder. When reconstituting with phosphate buffer pH 7.2 the active enzyme is obtained. To check its purity, an electrophoresis is performed where a single band of approximately 70,000 molecular weight is observed. The solution with enzymatic activity was stored at 4ºC for later use. A few days later it was found that the enzymatic activity had been lost and in the electrophoretic analysis, instead of a single band there were three bands of weights 40,000, 20,000 and 10,000. Come up with a reasoned explanation of what might have happened to the enzyme
Given this research scenarios kindly construct a research framework. A researcher is interested to test the antibacterial activity of a Philippine Plant crude extracts against Beta-lactamase producing Klebsiella pneumonia isolated in a hospital setting. He will use the following concentrations of crude extract, 500mg/ml, 250mg/ml and 100mg/ml. Positive control: Tetracycline 10mg/ml and DMSO as the negative control.
Pyridoxal phosphate (PLP) is a coenzyme for the enzyme ornithine aminotransferase. The enzyme was purified from cells grow in PLP = deficient media as well as from cells grown in media that contained pyridoxal phosphate. The stability of the two different enzyme preparations was then measured by incubating the enzyme at 37°C for different lengths of time and then assaying for the amount of enzyme activity remaining. The following results were obtained. (a) Why does the amount of active enzyme decrease with the time of incubation? (b) Why does the amount of enzyme from the PLP deficient cells decline more rapidly?
Provide an example of covalent catalysis in the mechanism of chymotrypsin. What is the nucleophile involved in the formation of this covalent bond? What enabled this group to become a good nucleophile?
A schematic representation of the enzyme IspD complexed to inhibitor 3, and a series of inhibitors 3-5 are shown below. Ala202 lle240 mwww NH NH Val263 ОН www HN N- lle177 HN 'N' CI 3 X = N 4 X = C-CN 5 X = C-COO IC50 274 µM IC50 140 nM IC50 35 nM NH2 HN Val266 N -N O-H---- N HN %3D Arg157 HN wwww lle265 Explain why structure 4 is a more potent inhibitor (lower IC50 value) than inhibitor 3 and why structure 5 is a much weaker inhibitor (higher IC50 value) than 3 and 4.
There is a cysteine protease, which uses a similar chemical mechanism to chymotrypsin except for using cysteine instead of serine during catalysis. Please draw the stepwise chemical mechanism for the cysteine protease.
It is required to recover active extracellular enzymes from a completed fermentation mediumthat also consists of proteins (<200,000 molecular weight cut-off (MWCO)) and bacterial cells (1-2μm). A cross-flow 0.35 μm microfiltration (MF) with retentate recycled back to the fermenter willbe used over a period of 5 hours during which time flux is assumed to decline linearly. After 5 hours, assuming 95% of the bacteria are retained and given the additionalinformation below, what is the concertation of bacteria remaining in the fermenter and what area,in m2 , of MF membrane is needed? Initial bacterial concentration = 1.2 gdcw /L (dcw = dry cell weight)Volume of medium at the beginning = 15 m3Volume of medium left in the fermenter after 5 hours filtering = 1 m3Initial (starting flux) = 6.5 x 10-5 m sec -1Final flux (after 5 hours of filtering) = 3.9 x 10-5 m sec -
A bacterial culture is grown using either octadecane (C18H38) or pentachlorophenol (C6HCl5O) as the sole source of carbon and energy. The cell yield value is determined by dry weight analysis to be 1.49 for octadecane and 0.05 for pentachlorophenol. Using either octadecane or pentachlorophenol, please describe the steps taken (and the final result) showing what percentage of the substrate carbon will be found as cell mass and as CO2? Please show all calculations.
Discuss the relationship between an organism’s ability to reducenitrate past the nitrite stage and that organism’s proteolyticactivity
Where do each of these 5 main themes occur in the chymotrypsin mechanism? 1) substrate specificity 2) induced fit 3) covalent catalysis 4) acid/base catalysis 5) transition state stabilization
A bacterial culture is grown using either octadecane (C18H38) or pentachlorophenol (C6HOCI5)) as the sole source of carbon and energy. The cell yield value is determined by dry weight analysis to be 1.49 for octadecane and 0.05 for pentachlorophenol. Using either octadecane or pentachlorophenol, please describe the steps taken (and the final result) showing what percentage of the substrate carbon will be found as cell mass and as CO2?
Staphylococcal nuclease has a ΔΔG‡ of -84.1 kJ mol-1 at 25.0 °C. If the uncatalyzed rate is 0.630x10-13 µmol s-1, calculate the enzyme-catalyzed rate in µmol s-1. (Use R = 8.3145 J mol-1 K-1)

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Basic Clinical Laboratory Techniques 6E

Biology

ISBN:

9781133893943

Author:

ESTRIDGE

Publisher:

Cengage

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Basic Clinical Laboratory Techniques 6E

Biology

ISBN:

9781133893943

Author:

ESTRIDGE

Publisher:

Cengage

SEE MORE TEXTBOOKS