Answer:
Michaelis constant is known as km which is the substrate concentration that encourages the compound to work at half maximum velocity represented by Vmax/2. Michaelis constant is inversely related to the substrate and the affinity of the enzyme.
Induced fit model: The premise of the purported induced fit hypothesis, which expresses that the attachment or association of a substrate or some other atom to an enzyme causes an adjustment to the enzyme in order to fit or restrain its activity.
In substrate, analog Km or Michaelis constant will be high as the substrate will stay because of analogs inhibit activity.
In the transitional state, analog Km will be in the middle of the substrate and product analogs. Progress state analogs are synthetic mixes with a structure catalyzed reaction that looks like the progressing condition of a substrate atom in a compound enzyme.
In item simple thus Km is the least.
0.0013 M = product ananlog,
0.025 M=Transition state, and
0.0045 M = Substrate analog
Answer:
35.5450 will be rounded to 35.55
Explanation:
=35.5450
if the last digit is less than 5 then it will be ignored
=35.545
when the dropping digit is 5 then the retaining digit will increse by a factor of 1
=35.55
i hope this will help you
Answer:
balanced
Explanation:
its balance since all the elments add up on both sides
Answer:
0.15M
Explanation:
The equation for molarity is M= n/L. Where "M" is Molarity, "n" is the number of moles of solute, and "L" is the total liters in solution.
You need to calculate the number of moles from the given grams. The molar mass of KOH is (39.098+ 16 +1.008)= 56.106g. To calculate the mols of KOH,
×
= 0.44558... mol, you see that the grams unit cancel out leaving you with mol as the unit.
The volume is given in L already so no need to do any conversion. M=
= 0.1485M ≈ 0.15M
Answer:
it is actually b because i did this i picked b and got it right
Explanation: