Which of the following is the correct value of the Kö?a.It is [substrate] at half VmaxO b. It is [substrate] at VmaxOc. It is half of the [enzyme]Od. It is half of the Vmax

Michaelis Menten Equation is given as v=Vmax[S]Km+[S] Here, v is the Initial reaction velocity…

Answered: Which of the following is the correct…

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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When measuring reaction velocity as a function of substrate concentration, a researcher usually keeps the concentration of enzyme at a constant level. What would happen if the enzyme concentration were not kept constant? A. Vmax would change, but Km would remain constant. B. Both Vmax and Km would change C. Vmax would remain constant, but Km would change D. Vmax would remain constant, but V would change E. None of the above would necessarily occur
A plot of 1½5 venut VSL, Glld a Br-weaver Burk or double-reciprocal plot, is a useful tool for identifying the type of Madily each gaph by dragging the endpoints to show the various types of enzyme inhibition. What is the inhibition mechanism for the competitive inhibitor? The inhibisr binde cenly in recemyne The inhibitor bindx only lo cozyme- substrate complexe The inhibike binds tas bath free enzyme and enzyme xubxirale completes with identical binding axolante. The inhibikr binds to both free enzyme and cozyme substrate completes with different binding constants. What is the inhibition mechaniam for the uncompetitive inhibitor? The inhibitor binds only to free ENZYMES. The inhibitor bind is both tree enzyme and enzyme auhdraic compleaca with identical binding coulants. The inhibar binds only in enzyme ubrale complex.ca. The inhibir bindis in bath free enzyme and cxyme aubairale complicaca with dill crcnt binding costanix. LAST Nompumps dve shk with inbibus WHEY Pullie mechanism kot…
The representative reaction of the enzymatic process is:
Suppose we have 2 proteins A and B with the following kcat and Km values. kcat (s) Km (uM) Prot. A 5.4x10 Prot. B 6.8x10 4,000 50 Which enzyme is the more efficient one?
WHICH OPTIN IS TRUE QUICK I WILL RATE NO EXPLANATION NEEDED
There is an enzyme inhibition mechanism that is not too detrimental when viewed from the size of Km, namely the inhibition mechanism.... A. non-competitiveB. non-competitive and uncompetitiveC. in-competitive and uncompetitiveD. in-competitiveE. uncompetitive
1. The most commonly used method in measuring LD because it produces a positive rate (NADH) and not affected by product inhibition a. Oliver-Rosalki b. Wrecker Method c. Wroblewski Ladue d. Tanzer-Gilbarg 2. most chemistry enzyme tests follow the zero order reaction where the sufficient amount of substrate is availbale the only limiting factor is the enzyme's substrate a. first statement is true and second statement is false b. both statements are true c. first statement is false and second statement is true d. both statements are true 3. any absorbance change per minute of activity when exceeds must be a. double the measurement and analyze again b. repeat analysis c. discared the reagent and open new one d. dilute sample and repeat analysis and multiply the dilution
When substrate concentration [S] << Km, the rate of an enzymatic reaction is increased by O increasing kcat/Km O increasing total enzyme concentration O increasing [S] O A and B O A, B and C
Which phrase characterizes a uncompetitive inhibitor? OA. binds either enzyme or enzyme-substrate complex when present, Km of an enzyme will appear to decrease OB. when present, Km of an enzyme will either increase or decrease when present, Km of an enzyme will appear to increase OD.
Here’s a kinetic model for some enzyme E acting on substrate S. Give the equation for the change in the concentration of free enzyme (E) with time.
Determine the Vo as a function of Vmax when the substrate concentration is equal to 10 KM or 20 KM. What does this tell you about an enzyme ability to reach Vmax?

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Which of the following is the correct value of the KM? a. It is [substrate] at half Vmax b. It is [substrate] at Vmax c. It is half of the [enzyme] Od. It is half of the V. max