Question

Theory of enzymes. [Indicate whether the following statements are true or false by writing T or F in the spaces provided.] _____ Enzymes catalyze reactions by increasing the reaction free energy (ΔG). _____ Enzyme are remarkable for their substrate specificity. _____ Enzyme can convert light energy into chemical or mechanical energy. _____ Catalytic residues in enzymes can include amino acid side chains, RNA bases, and other organic cofactors. _____ Michaelis-Menten kinetic theory only applies to enzymes with single substrates. _____ Enzymes bind transition-state analogs more tightly than substrates. _____ At high substrate concentration, reactions are rate-limited by how rapidly enzymes convert substrates into products. _____ KM = KD when kcat >> k-1 _____ kcat / KM is equivalent to a second-order rate constant. _____ Enzymes can use electrostatics to exceed the rate of diffusion (bimolecular collision of substrate with enzyme’s active site). _____ Drugs that bind to an allosteric site on an enzyme cause a decrease in kcat

Answer 1

Theory of enzymes. [Indicate whether the following statements are true or false by writing T or F in the spaces provided.]

___ F__ Enzymes catalyze reactions by increasing the reaction free energy (ΔG).

__T___ Enzyme are remarkable for their substrate specificity.

F_____ Enzyme can convert light energy into chemical or mechanical energy.

T_____ Catalytic residues in enzymes can include amino acid side chains, RNA bases, and other organic cofactors. _T____ Michaelis-Menten kinetic theory only applies to enzymes with single substrates.

F_____ Enzymes bind transition-state analogs more tightly than substrates.

T_____ At high substrate concentration, reactions are rate-limited by how rapidly enzymes convert substrates into products.

F_____ KM = KD when kcat >> k-1 _____ kcat / KM is equivalent to a second-order rate constant.

F_____ Enzymes can use electrostatics to exceed the rate of diffusion (bimolecular collision of substrate with enzyme’s active site).

T_____ Drugs that bind to an allosteric site on an enzyme cause a decrease in kcat