Yarrowia lipolytica(Yl) is a non-conventional yeast that diverged from baker’s yeast, Saccharomyces cerevisiae(Sc), early in evolutionary history. The regulation of glycolytic enzymes in Yl differs from that of Sc. The data below pertain to regulation of phosphofructokinase 1 (PFK). Data for Yl is shown with black circles and data for Sc is shown with white circles.Imagine that the genes for phosphofructose kinase 2 and fructose 2,6-bisphosphatase were deleted in each species. Which species would you expect to have greater metabolic disruption and why? ### Graph Analysis: Regulation of PFK Activity#### Figure 1: Effect of Fructose-2,6-P2 on PFK ActivityThe graph on the left displays the relative activity of phosphofructokinase (PFK) from two different species, referred to as YIPfk and ScPfK, as a function of Fructose-2,6-P2 concentration, measured in micromoles (µM).- **X-axis (Horizontal):** Indicates the concentration of Fructose-2,6-P2 (µM), ranging from 0 to 100 µM.- **Y-axis (Vertical):** Shows the relative activity of PFK, where 1.0 represents the maximum activity.**Observations:**- The solid circles represent YIPfk activity, which remains high and constant at 1.0 relative activity across the range of Fructose-2,6-P2 concentrations.- The open circles represent ScPfK activity, which shows a steep increase in relative activity at lower concentrations, reaching a plateau near 0.8 relative activity at around 10 µM Fructose-2,6-P2, and then remaining steady.#### Figure 2: Effect of P-Enolpyruvate on PFK ActivityThe graph on the right illustrates the relative activity of PFK from the same two species (YIPfk and ScPfK) as a function of Phosphoenolpyruvate (P-enolpyruvate) concentration, measured in millimoles (mM).- **X-axis (Horizontal):** Shows the concentration of P-enolpyruvate (mM), ranging from 0 to 10 mM.- **Y-axis (Vertical):** Represents the relative activity of PFK, using the same scale as the previous graph.**Observations:**- The solid circles represent YIPfk activity, which shows a rapid decline in activity with increasing P-enolpyruvate concentration, nearing zero at around 2 mM and staying low thereafter.- The open circles represent ScPfK activity, showing a gradual decrease in relative activity to about 0.2 as P-enolpyruvate concentration increases to 10 mM.### ConclusionThese graphs demonstrate the regulatory effects of Fructose-2,6-P2 and P-enolpyruvate on PFK activity from different species. Fructose-2 ### Enzyme Kinetics: Relative Activity of Phosphofructokinase (PfK) in Response to Fructose-6-Phosphate (Fructose-6-P) ConcentrationThis graph illustrates the relative activity of two variants of phosphofructokinase (PfK) enzymes, labeled as YlPfK and ScPfK, in response to varying concentrations of fructose-6-phosphate (Fructose-6-P).**Axes:**- The **x-axis** represents the concentration of Fructose-6-Phosphate (Fructose-6-P) in millimoles per liter (mM), ranging from 0 to 10 mM.- The **y-axis** indicates the relative activity of PfK, normalized and denoted as v/V₁, ranging from 0.2 to 1.0 with tick marks at intervals of 0.2.**Data Points and Curves:**- Two sets of data points are plotted: - **YlPfK** is represented by filled black circles (●). - **ScPfK** is depicted using open circles (○).**Trends and Observations:**- For lower concentrations of Fructose-6-P (0-2 mM), YlPfK demonstrates an initial rapid increase in relative activity, reaching a relative activity close to 0.8 at around 2 mM and leveling off as it approaches concentrations between 4-6 mM.- ScPfK shows a more gradual increase in activity compared to YlPfK. At around 2 mM, it achieves a relative activity of approximately 0.6, and it continues to gradually increase to a maximum activity close to 0.8 at Fructose-6-P concentrations between 4-6 mM.- Beyond 6 mM concentration of Fructose-6-P, the relative activity of both YlPfK and ScPfK plateaus, indicating that further increases in Fructose-6-P do not significantly enhance enzyme activity.This graph provides vital insight into the enzyme kinetics of two variants of phosphofructokinase in the presence of its substrate, Fructose-6-Phosphate. It suggests that YlPfK might reach its maximum activity faster than ScPfK, but both plateau at similar activity levels. Understanding such behaviors is essential for biochemical applications and research

Yarrowia lipolytica (Yl) of PFK-2 is highly suspect in allosteric changes in graph than compared of…

Answered: Yarrowia lipolytica(Yl) is a…

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...