Use the Michael is-Menten equation to complete the enzyme kinetic data set, when

Question

Use the Michael is-Menten equation to complete the enzyme kinetic data set, when K_m is known to have a value of 1 mmol/L. Fill-in-the-blank questions: Organic cofactors are referred to as The difference in values for Delta G and Delta G degree is in the One way to measure the rate of an enzymatic reaction is to measure the loss of over time. The Michaelis-Menten model assumes that is the rate constant ignored because P has not accumulated. The effect stabilizes the structure of DNA, resulting in more polar surfaces being exposed to the aqueous media.

Explanation / Answer

1. We know that, Vo=Vmax(S)/Km+S

Then, convert all the values into micromoles, Km-1mmol/L, i.e. 1000 micromoles/L

Substrate-0.5 mol/L i.e. 500 mmol/L or 500000 micromole/L, 1 mol/L i.e. 1000 mmol/L or 1000000 micromole/L

like that for for 2, 3 and 10 mol/L i.e. 2000000 micromole/L, 3000000 micromol/L, and 10000000 micromoles/L respectively.

Vo is 50 micromole/L/min

Now need to calculate Vmax, so individual values to be substituted into above equation

1.a. 50=Vmax(500000)/1000+500000, then Vmax is 50.1 micromole/L/min, Hence, I/2 Vmax would be 25.05 micromole/L/min

1.b. 50=Vmax (1000000)/1000+1000000, Vmax is 50.05 micromole/L/min, Hence, I/2 Vmax would be 25.025 micromole/L/min

1.c. 50=Vmax (2000000)/1000+2000000, Vmax is 50.025 micromole/L/min, Hence, I/2 Vmax would be 25.0125 micromole/L/min

1.d 50=Vmax (3000000)/1000+3000000, Vmax is 50.016 micromole/L/min, Hence, I/2 Vmax would be 25.00833 micromole/L/min

1.e 50=Vmax (10000000)/1000+10000000, Vmax is 50.005 micromole/L/min, Hence, I/2 Vmax would be 25.0025 micromole/L/min

2. a. coenzyme

b. The condition of the reaction i.e. at standard study state conditions (delta-G0) at any condition either forward or reversible or equilibrium (delta-G) could be the difference.

c. substrate

d. Rate constant is a characteristic of the strength of ES complex, if ignored there will no product formation

e. Hydrophobic effect by hydrogen bonding inside the helix

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