Kcat= 30.0sec^-1
Km= 0.0050M
Total enzyme Concentration= 1uM
What is the max rate of the enzyme?
Kcat = Vmax/Et
Kcat = 30
Vmax = ?
Et = 1 × 10^-6
30 = Vmax/10^-6
Vmax = 30 × 10^6 = 3 × 10^7 M per second
Vmax = maximum velocity of an enzyme catalysed reaction
Km = substrate concentration at which the velocity of the reaction is half of Vmax
Kcat is turnover number, number of substrate molecules converted to products by one active site of enzyme at a given time
Please rate high.
Kcat= 30.0sec^-1 Km= 0.0050M Total enzyme Concentration= 1uM What is the max rate of the enzyme?
54. What is the catalyze reaction rate? Km=2 mM Kcat= 3 s-1 At the enzyme concentration=10 nM and substrate concentration= 3 mM
At what substrate concentration would an enzyme with a kcat of 30.0 sec-1 and a Km of 0.0030 M have an initial velocity that is 25% of the maximum velocity? a. 0.0010M b 0.0090 M c. 0.0015 M d. 0.0060 M e.Cannot be determined
At what substrate concentration would an enzyme with a kcat of 30.0 sec-1 and a Km of 0.0030 M have an initial velocity that is 25% of the maximum velocity? a. 0.0010M b 0.0090 M c. 0.0015 M d. 0.0060 M e.Cannot be determined
Does increasing enzyme concentration changes the value of Vmax, Km and Kcat? Why?
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Given the enzyme system just described (Km = 8.20*10-5M and kcat = 40.0 s-1, [Eltot = 2.00*10-7 M), suppose we introduce a classical noncompetitive inhibitor with K1 = 1.20*10-7M. If the concentration of inhibitor introduced is 3.0 um, what will the effective kcat be? Express your answer in s-1.
Glucokinase is a liver enzyme with a kcat of 33/second and a Km for Glucose of 7 mM. What is the initial reaction rate (in mM product / second) of 0.1 mM glucokinase in the presence of 50 mM glucose? Please show your work clearly.