Triose phosphate isomerase follows Michaelis-Menten kinetics. A
1.7 micromolar solution of triose phosphate isomerase has a
kcat of 706 s-1 when converting
glyceraldehyde-3-phosphate to dihydroxyacetone phosphate. What is
triose phosphate isomerase's Vmax with
glyceraldehyde-3-phosphate?
12 M-1 s-1
0.415 mmoles s-1
1.2 mmoles s-1
1.2 x 104 M-1 s-1
0.0024 moles s-1
Kcat= Vmax/ [ET]
[ET]= total enzyme concentration = 1.7 micromolar
Kcat= 706 s-1
[E] = 1.7 micromolar
Vmax= Kcat X [E]
Vmax= 706 s-1 X 1.7 micromolar = 1200.2 micromolar s-1
1 micromolar=0.001 mmol
Vmax= 1200.2 micromolar s-1 X 0.001 mmol= 1.2 mmol s-1 = 1.2 mmol/s
Right choice= 1.2 mmoles s-1
Triose phosphate isomerase follows Michaelis-Menten kinetics. A 1.7 micromolar solution of triose phosphate isomerase has a...
Triose phosphate isomerase follows Michaelis-Menten kinetics. A 1.7 micromolar solution of triose phosphate isomerase has a Kcat of 706 s-1 when converting glyceraldehyde-3-phosphate to dihydroxyacetone phosphate. What is triose phosphate isomerase''s Vmax with glyceraldehyde-3-phosphate? a) 12 M-1 s-1 b) 1.2 mmoles s-1 c) 0.0024 moles s-1 d) 0.415 mmoles s-1 3) 1.2 X 10^4 M-1 s-1
An enzyme that follows Michaelis-Menten kinetics has a KM value of 20.0 μM and a kcat value of 211 s−1. At an initial enzyme concentration of 0.0100 μM, the initial reaction velocity was found to be 1.07×10−6 μM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures.
Part A An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 uM and a kcat value of 201 s-1. At an initial enzyme concentration of 0.0100 uM, the initial reaction velocity was found to be 1.07 x 10- uM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures. ► View Available Hint(s) PO ALO O O ? [S]; = MM UM
13. Explain this statement: An Enzyme follows Michaelis-Menten kinetics, meaning explain the characteristics of a M-Menzyme and the type of mechanism it uses. Also, include definitions of Km and Vmax. (This is that synthesis question.) 14. Compare and contrast E-S interactions with P-L interactions.
4. Basic concepts of Michaelis-Menten kinetics. The Michaelis-Menten equation is expression of the relationship between the initial velocity, Vo, of an enzymatic reaction and substrate concentration, [S]. There are three conditions that are useful for simplifying the Michaelis-Menten equation: [S] <<Km; [S] = Km; [S] >> Km. Match each condition with the statement(s) that describe it. TV, Vmox[S] Vo =Vmax m . V Vo - Vmax [S] Km +[S] V. (um/min) max [S] (mm) (a) Doubling [S] will almost double...
A single-substrate enzyme that obeys Michaelis-Menten kinetics displays the following parameters: Kd = 3.1 x 10^-5 M; k1 = 107 M-1 s-1, and kcat = 10^4 s-1. Given this information, what is the value of the Michaelis constant Km? Express your answer in terms of mM to four significant figures.
An enzyme that follows Michaelis-Menten kinetics has a initial velocity of 300 nM/s at a substrate concentration of 30 uM. The maximum velocity of 400 nM/sec. What is the Km for this enzyme in uM? (Give your answer as a number only. Type your response
Assuming that an enzyme catalyzed reaction follows Michaelis-Menten kinetics with a Km of 1 x 10-6 M. If the initial reaction rate (V0) is 0.1 μmol/min at 0.1 M, what would it be at 0.01 M, 10-3M, and 10-6 M?
2) (5 marks) The enzyme Happyase follows simple Michaelis – Menten Kinetics a. The Km of Happyase for its substrate ICE is Km^s = 1mM. Happyase also acts on substrate CREAM and its Km^T =10mM. Is ICE or CREAM the preferred substrate for Happyase? Explain b. The rate constant k2 with substrate ICE is 2x10^4sec^ -1; with substrate CREAM, k2=4x10^5sec ^-1. Does Happyase use substrate ICE or substrate CREAM with greater catalytic efficiency? Show calculations and explain your answer
This is a Biochemistry 200 level question, please answer neatly
and as soon as possible. Thank you!
QUESTION 2 The kinetics parameters of several enzymes are listed below. Arrange the enzymes in order of decreasing catalytic efficiency. Enzyme Substrate kcat (s-1 Km Triosephosphate isomerase Glyceraldehyde-3-phosphate 4.3 x 103 0.47 mm Catalase H202 1.1 M Fumarase fumarate 5.0 x 10-6 M 4.0 x 107 8.0 x 102 5.7 x 103 1.0 x 106 Crotonase crotonyl-CoA 2.0 x 10-2 mm 1.2 x...