Answer: Km = 10μM
Explanation: <u>Michaelis-Menten constant</u> (Km) measures the affinity a enzyme has to its substrate, so it can be known how well an enzyme is suited to the substrate being used. To determine Km another value associated to an eznyme is important: <em>Turnover number (Kcat)</em>, which is the number of time an enzyme site converts substrate into product per unit time.
Enzyme veolcity is calculated as:
![V_{0} = \frac{E_{t}.K_{cat}.[substrate]}{K_{m}+[substrate]}](https://tex.z-dn.net/?f=V_%7B0%7D%20%3D%20%5Cfrac%7BE_%7Bt%7D.K_%7Bcat%7D.%5Bsubstrate%5D%7D%7BK_%7Bm%7D%2B%5Bsubstrate%5D%7D)
where Et is concentration of enzyme catalitic sites and has to have the same unit as velocity of enzyme, so Et = 20nM = 0.02μM;
To calculate Km:
![V_{0}*K_{m} + V_{0}*[substrate] = E_{t}.K_{cat}.[substrate]](https://tex.z-dn.net/?f=V_%7B0%7D%2AK_%7Bm%7D%20%2B%20V_%7B0%7D%2A%5Bsubstrate%5D%20%3D%20E_%7Bt%7D.K_%7Bcat%7D.%5Bsubstrate%5D)
![K_{m} = \frac{E_{t}.K_{cat}.[substrate]-V_{0}*[substrate]}{V_{0}}](https://tex.z-dn.net/?f=K_%7Bm%7D%20%3D%20%5Cfrac%7BE_%7Bt%7D.K_%7Bcat%7D.%5Bsubstrate%5D-V_%7B0%7D%2A%5Bsubstrate%5D%7D%7BV_%7B0%7D%7D)
Km = 10μM
<u>The Michaelis-Menten for the substrate SAD is </u><u>10μM</u><u>.</u>
Answer:
Trough is the lower bound of wave, while the crest is the upper bound of a wave.
Explanation:
see picture attatched
2Al + 6HCl ----> 2AlCl3 + 3H2
Explanation:
<u>Periodic table is the tabular display of elements that are arranged by the increasing atomic number.
</u>
Structure of the periodic table shows various periodic trends.
<u>Significance:
</u>
The periodic table is very important because it gives an organized way to provide lots of information about the elements and how they can be related to one another. The table gives a systematic approach to study the elements and their properties. The table can also be used to predict the properties of the elements which have not been discovered yet.
