True or FalseEnzymes topic SMART VOLTEOON 47)1 5:15No serviceThe rate of an enzyme-catalyzed reaction increasesas the temperature is raisedbeyond optimumtemperature.Many enzymes require thepresence of othercompounds - cofactors -before their catalytic activitycan be exerted.if the amount of the enzymeis kept constant and thesubstrate concentration isthen gradually increased, thereaction velocity willdecrease.In the Induced-fit Model, if adissimilar substance whichdoes not fit the site ispresent, the enzyme rejects itOxidases change thegeometry of a moleculeA prosthetic group - anorganic substance which isdialyzable and thermostablewhich is firmly attached tothe protein or apoenzymeportion.The enzyme is thought tolengthen the "path" of thereaction.Absolute specificity will actonly on molecules that havespecific functional groups.Beyond maximum velocity,increasing the amount ofsubstrate in the system,while the enzymeconcentration is constant,will further increase theenzyme activity.Enzyme inhibitors aresubstances which eitherincrease or decrease thecatalytic action of theenzyme.(

Answered: Image /qna-images/answer/12a1c4ed-2cd7-4078-8954-42558bda01ad.jpg

The rate of an enzyme- catalyzed reaction increases as the temperature is raised beyond optimum temperature. Many enzymes require the presence of other compounds - cofactors - before their catalytic activity can be exerted. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme reiects it

The rate of an enzyme- catalyzed reaction increases as the temperature is raised beyond optimum temperature. Many enzymes require the presence of other compounds - cofactors - before their catalytic activity can be exerted. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme reiects it

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

See similar textbooks

Similar questions

In the rete mirabile serving the red swimming muscles oftunas, some key enzymes of catabolism show gradients ofconcentration: They are more concentrated at the cold end of therete, and less concentrated at the warm end. These variationsparallel variations that are often seen in the thermal acclimationof poikilotherms, when enzyme concentrations rise duringacclimation to cold and fall during acclimation to heat. Whatdo you think could be some of the reasons for these spatial andtemporal variations in enzyme concentration? Why not havethe highest observed enzyme concentrations everywhere at alltimes?
3D 40 50 70 10m 11 120 14 130 150 160 17 18 19 20 28M 29 300 31 320 330 Julass ierIses in igL TTTCrOSCopes reiract 1igrit, wrichTreautes resolutiorn. QUESTION 31 Explain what the active site of an enzyme is. Name and describe three mechanisms used by the cell for regulating enzyme activity (use the term "active site" in your description of each). Paragraph 3 (12pt) 只i :公 TTTT Arial HTML CSS fx Mashups 囲 Words:0 Path: p QUESTION 32 QIXA Describe the mechanism of the sodium/potassium pump and why it is important to the function of the cell? For the toolbar, press ALT+F10 (PC) or ALT+FN+F10 (Mac), 3 (12pt) LT Arial
If you graph the velocity of an enzymecatalyzed reaction vs. [S] for each of two substrates that are partof a random mechanism, would you expect to see the same shapecurve? Why or why not?
Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)
126 nmol of enzyme catalyzes the conversion of 2.8 ugram of substrate (molar mass- 350 g/mol) in t second at 37C at Vman what is the turnover number kcat for the enzyme in units of s R Show all your work to recenve credit. For the toolbar, press ALTF10 (P) or ALTFNF10 (Mac). %3B .... BIUS Paragraph Arial 14px
ANN/ SUAMF 2. (a) Fig. 2.1 shows the effect of temperature on the activity of enzyme E. rate of activity/ arbitrary units 40 60 80 100 temperature/C Fig. 2.1 () State the optimum temperature for enzyme E (i1) Suggest a possible identity for enzyme E, where it is found, and its function. identity of enzyme E where it is found function on the activity of another enzyme, F
3:43 ll LTE O moellim.riphah.edu.pk Biochemistry-l Dashboard / My courses / Biochemistry-II | General / QUIZ 1 Question 7 Not yet answered Marked out of 1.00 P Flag question ADP will the regulatory enzymes of TCA cycle? Select one: O a. None O b. Both depending on condition O c. Inhibit O d. Activate Next page Course Outline
What enzyme kinetic parameters are apparantly impacted by uncompetitive inhibitors? Vmax Km Both Km and Vmax Neither Km nor Vmax
WMapp E+S ES E+P Vmax Km =Vmax 2 -1 a = 1+ [1]/K, X intercept = Kcat [E]T Km Question 6 In the simple enzyme-catalyzed reaction below, which of the rate constants would be second-order? E+S ES →E+P k-1 O k2 O k-1 O k1
Enzymes act by reducing the activation energy of areaction. Describe several ways in which this isaccomplished.
1 pt pt 9146 Bb 9146 Bb 1031 Class Etsy E Traps E Traps New Free Chat + ☆ 出口 keAssignment/takeCovalentActivity.do?locator-assignment-take [References] You do an enzyme kinetic experiment and calculate a Vmax of 118 μmol per minute. If each assay used 0.10 mL of an enzyme solution that had a concentration of 0.20 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol? (Enter your answer to two significant figures.) turnover number = sec-1 D 1 pt Submit Answer Try Another Version 2 item attempts remaining estion stion 5 on 6 7 1pt 1 pt 1 pt 1pt 1pt 1pt 1 pt 1 pt D is the substrate concentration multiplied by the catalytic constant. KM is equivalent to the substrate concentration multiplied by the ratio of rate constants for the formation and dissociation of the enzyme-substrate complex. KM is equivalent to the substrate concentration. KM is equivalent to the substrate concentration divided by 2 A: KM is equivalent to the substrate concentration…
PART IV. HOW FAST DOES IT GO?Another member of your research group studied the kinetics of theGAPDH from the organism. They also determined if the GAPDH fromthe organism is also inhibited by the known inhibitor of GAPDH fromhumans. A. From the following data, determine the KM (Michaelis-Menten Constant) and the Vmax(maximum velocity) of the enzyme without and with the inhibitor. B. If GAPDH is inhibited, what specific type of inhibition is observed?