The michaelis-menten equation is an expression of the relationship between the initial velocity, v0, of an enzymatic reaction and substrate concentration, [s]. there are three conditions that are useful for simplifying the michaelis-menten equation to an expression from which the effect of [s] on the rate can be more readily determined. match the condition (e. g. [s] = km) with the statement(s) that describe it:

1. doubling [s] will almost double the rate.
2. half of the active sites are occupied by substrate.
3. about 90% of the active sites are occupied by substrate.
4. doubling [s] will have little effect on the rate.
5. less than 10% of the active sites are occupied by substrate.
6. this condition will result in the highest rate.

Option 2, Half of the active sites are occupied by substrate

Explanation:

Michaelis-Menten expression for enzyme catalysed equation is as follows:

Here, is Michaelis-Menten constant and [S] is substrate concentration.

When [S]=Km

Rearrange the above equation as follows:

when [S]=Km, the rate of enzyme catalysed reaction becomes half of the maximum rate, that means half of the active sites are occupied by substrate.

Therefore, the correct option is option 2.

hope this

explanation:

covalent bonds

consist of pairs of electrons shared by two atoms, and bind the atoms to fixed orientation and requre high energies to break them

ionic bonds

when two atoms differ considerably in their electronegativity, then one of the atoms will lose its electron to the other atom. this results in a positively charged ion(cation) and a negatively charged ion (anion)

they it depends on if one believes about radioactivity, they make a geiger counter beep but maybe it was going to beep anyway electronics do wierd things all the time or it was programmed to beep near certain metals.