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
= 3.14 × 10 with the power of 0
(scientific notation)
= 3.14e0
(scientific e notation)
= 3.14 × 100
(engineering notation)
(one)
= 3.14
(real number)
I think because each element has its own number of protons and neutrons, giving it its own atomic number and mass (correct me if I’m wrong please)
This is the same as its freezing point
hope this helps
