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: 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?

Answer to kcat/KM can never be greater than O ki O k-1+k2 O. This AI-generated tip is based on Chegg's full solution.

2.1.The ratio kcat/KM – often referred to as the 'specificity constant' – is a useful index for comparing the relative rates of an enzyme acting on alternative, competing substrates. At high substrate concentrations, kcat is the parameter that best d …View the full answer

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 Your solution’s ready to go!

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 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 <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.

Velocity is expressed in uM/sec and the total concentration of each enzyme is 2.9 nM. Be sure to show your work. Enzyme α Vmax KM kcat kcat/Kw 1/[S] (uM-1) Enzyme β Vmax- KM kcat kcat/KM 4 2 0 2 4 6 8 10 1/IS] (uM1) Enzyme γ Vmax kcat kcat/KM 14-12-10-8 6 4 2 02 4 6 8 10 1/[S] (uM1) Determine which Enzyme is the most efficient?

Question: (5 of 5) The keap/Km ratio of acetyl cholinesterase is 1.6x108M''sl, and the kcat/km of fumarase is 1.6x108 Milsl. From this information which of the following can you conclude? These two enzymes require similar concentration of substrate to reach Vmax • At saturating conditions these two enzymes are equally efficient.

The pH can have an effect on Kcat/Km. Kcat/Km is a ratio which indicates the catalytic efficiency of an enzyme. It is sensitive to pH because enzyme... Become a member and unlock all Study Answers