a) it looses its native conformation

b) its peptide bond are broken

c) enzyme solubility increases

d) it can still binds its substrate and catalyze the reaction

a) velocity before adding the enzyme

b) velocity before accumulation of product

c) velocity at zero substrate concentration

d) velocity with substrate concentration equal to Km

e) the lowest velocity

a) increase km with no change in Vmax

b) decrease km and Vmax

c) increase Vmax with no change in km

d) decrease Vmax with no change in km

a) the protein part of an enzyme

b) an inactive enzyme

c) an inorganic cofactor

d) a substrate needed for the enzyme action

a) forcing the reaction against natural equilibrium

b) lowering the activation energy of the reaction

c) binding the products of the reaction to guarantee its continuity

d) giving the reactants energy required to make the reaction

a) half the substrate concentration that gives Vmax

b) the substrate concentration that half saturate the enzyme

c) the initial velocity at half saturation of the enzyme

d) none of the above

a) increased km with no change in Vmax

b) decreased km and Vmax

c) no change in km and decreased Vmax

increased km and decreased Vmax

a) increased synthesizes of the enzyme from the gene

b) increased kinetic energy of the enzyme

c) activation of an inactive enzyme

d) enhanced affinity between the enzyme and its substrate

a) decrease formation of uric acid

b) decreases Vmax and no change in km

c) the effect can not be reversed by dialysis

d) the effect can not be reversed by increasing substrate concentration

e) all of the above

a) can bind covalently to the enzyme

b) can bind to the active site of the enzyme

c) binds non covalently to the enzyme

d) is derived from a vitamine

a) the substrate

b) the competitive enzyme

c) the coenzynme

d) the allosteric molecule

e) none of the above

a) hydrolyases

b) ligases

c) lyases

d) transferases