G In the absence of allosteric effectors, the enzyme phosphofructokinase displays Michaelis–Menten kinetics (see Fig. 7.15). The v0/Vmax ratio is 0.90 when the concentration of the substrate, fructose-6-phosphate, is 0.10 mM. Calculate the KM for phosphofructokinase under these conditions (in units of mM).

The value of the Michaelis–Menten constant is 0.0111 mM.

Explanation:

Michaelis–Menten 's equation:

Where:

= rate of formation of products

[S] = Concatenation of substrate

=  Michaelis constant

 = Maximum rate achieved

= Catalytic rate of the system

= Initial concentration of enzyme

On substituting all the given values

We have :

[S] = 0.10 mM

The value of the Michaelis–Menten constant is 0.0111 mM.

substituting a hydrogen atom with a halogen in a hydrocarbon:

- the single bond remains single. a is wrong.

- the bond with hydrogen is as strong as with a halogen. c is wrong

- a hydrocarbon is saturated if there is no double bond. we do not know that so d is wrong.

- carbon will always have four valence electrons. e is wrong.

by elimination, the correct answer is b. the boiling point of the new compound increases.

idk what is it? is this a question that you know the answer or u dont