Question

741) (5 pts) Transition state theory relates the rate constant to the free energy of activation, AG. How can enzymes reduce the activation energy barrier? a) decrease the free energy of the product b) high affinity binding to the transition state c) increase the free energy of the substrate d) increase entropy upon release of product e) bind to the substrate with high affinity 2) (5 pts) Which is true for a transition state analog? (select all correct answers) a) bound by weak non-covalent interactions b) decreases maximum reaction rate (Vmax) of the enzyme c) used to elucidate the catalytic mecahnism d) uncompetitive inhibitor of enzyme activity inhibitor of enzyme activity e) binds with higher affinity than substrate 3) (6 pts) Which amino acid sidechains can serve as a general acid or base catalyst? (select all correct answers) 510, AS a) aspartate d) histidine (b) serine e) isoleucine 7c) glutamine f) lysine CUS Mis 4) (5 pts) What is the role of the zinc ion cofactor in carbonic anhydrase? a) binds both water and carbon dioxide in the correct orientation b) activation of water to produce a nucleophilic hydroxide ion c) electrostatic catalysis that stabilizes the bicarbonate ion d) transfers an electron to carbon dioxide to generate bicarbonate e) binds carbon dioxide in the bent conformation of the transition state Vmax [S] KM + [S] VS) (5 pts) What is the "steady-state" assumption in the Michaelis-Menten equation? a) enzyme binding to substrate is in rapid equilibrium with dissociation b) the Michaelis constant, Km, is equivalent to the dissociation constant c) the concentration of the enzyme-substrate complex is unchanged d) release of product is the rate limiting step in enzyme kinetics e) the initial velocity is only dependent on the enzyme concentration

biochemistry
if you could please help me answer the following questions!

Answer 1

Ans 1 : e) bind to the substrate with high affinity

Enzymes are the biological catalysts of our body that increase the rate of biochemical reactions.

These enzyme molecules bind to the substrate with high affinity such that the activation energy barrier of the reaction decreases.

So better binding of the substrate into active sites of enzyme facilitates the reaction and cause it to proceed with a faster rate.