Question: Which one of the following statements about Km is FALSE:Group of answer choicesThe specificity constant kcat/Km reflects both binding and catalytic event, therefore, it can be used to compare enzyme preferrences for different substrate.Km reflects the binding affinity between an enzyme and a substrate.The higher the Km, the more efficient the enzyme is.Km

Question: 56. An enzyme's specificity constant (kcat/Km) has a maximum upper limit due to: A) substrate concentration.

Question: An enzyme is near maximum efficiency when O kcat/Km is near 108 M-15-1 its turnover number is near Vmax Oky<< k-1 OKM is large when k2 exceeds k1 Okcat/Km is equal to kcat Show transcribed image text

Question: Calculate kcat /KM for the enzyme reaction. Express your answer to two significant figures.Consider the enzyme-catalyzed reaction with Vmax=164(μmol/L)min−1 and KM=32 rmal/L. If the total enzyme concentration was 8zmol/L. how many molecules of substrate can a molecule of enzyme process in each minute?

C) kcat requires you to know the total enzyme concentration; kcat/KM does not require you to know the total enzyme concentration D) kcat applies only at substrate concentrations that can be achieved in a laboratory setting; kcat/KM applies at cellular concentrations of substrate E) kcat requires you to know the Vmax of the reaction under ...

The kcat / Km ratio of acetyl cholinesterase is 1.6 × 1 0 ∧ 8 M ∧ − 1 s ∧ − 1, and the kcat / Km of fumarase is 1.6 × 1 0 ∧ 8 M ∧ ⋅ 1 s ∧ ⋅ 1. From this information which of the following can you conclude? These two enzymes require similar concentration of substrate to reach 1/ V max. These two enzymes turnover numbers are ...

The enymatic rate constant (kcat/Km) of orotidine 5'-phosphate decarboxylase is 6 x 107 M-ls-1 and the nonenzymatic rate constant (kn) is 3 x 10-16 s-l. What is the value of the enzyme's catalytic proficiency?

What is the upper limit of the kcat/Km ratio? O a. Circe limits O b. diffusion-controlled rate O c no limit O d.

kcat/KM is approaching zero. The most efficient enzymes are characterized by the following value: K M is a ...

The specificity constant is equal to O a. Km/vo O b.kcat / [Et]. O c. [E+][S] /vo O d. kcat/Km QUESTION 2 For a given reaction with a AG &lt;0, the reaction is O a. unfavorable in both directions. O b. favorable in both directions. O c. favorable in the reverse direction. O d. favorable in the forward direction.