Effectors may show stimulatory or inhibitory activity. Binding one subunit impacts binding of substrate to other subunits. ALL are correct. The enzyme can have multiple subunits. The regulatory effect is by altering conformation and interaction of subunits.

Hello your question is poorly written below is the well written question

All are characteristic of allosteric enzymes except:

a. effectors may show stimulatory or inhibitory activity

b. they have multiple subunits

c. they obey Michaels-Menten kinetics

d. the regulatory effect is by altering conformation and interation of subunits

e. binding one subunit impacts binding of substrate to other units.

Answer : They Obey Michaels-Menten kinetics ( c )

Explanation:

Allosteric enzymes are enzymes that posses the presence of an additional site and an active site.  they are modified by a noncovalent binding an allosteric effector. They do not posses a kmvalue hence they do not obey Michaels-Menten kinetics

answer: glucoamylase presented optimum activity at temperature of 55â°c, and, in the glycosidic bonds from the non-reducing ends of starch, resulting in the production of glucose. source and type of fermentation can affect the enzyme's properties

credit to kalahira

the cells uses some of the atoms of the glucose molecules to atp molecules. the atoms of the glucose molecules will then be converted into energy which will be eventually stored in atp. the energy produced which are stored in atp are coming from the glucose’s chemical bonds.