Enzymes Before they can react, many molecules need to be destabilized. This state is typically achieved through changing the reaction from a biosynthetic to a catabolic pathway oxidizing the molecules by removing electrons the input of a small amount of activation energy changing the three-dimensional shape of the molecule changing the reaction from a biosynthetic to a catabolic pathway oxidizing the molecules by removing electrons the input of a small amount of activation energy changing the three-dimensional shape of the molecule ANSWER DOWNLOAD EXAMIANS APP
Enzymes In the enzyme-catalyzed reaction shown below, what will be the effect on substances A, B, C, and D of inactivating the enzyme labeled E2? A ---(E1)---> B ---(E2)---> C ---(E3)---> A, B, and C will still be produced, but not D A will still be produced, but not B, C, or D A, B, C, and D will all still be produced A and B will still be produced, but not C or D A, B, and C will still be produced, but not D A will still be produced, but not B, C, or D A, B, C, and D will all still be produced A and B will still be produced, but not C or D ANSWER DOWNLOAD EXAMIANS APP
Enzymes Tryprotophan synthetase of E.coli, a typical bifunctional oligomeric enzyme consist of a protein A and one-subunit a a protein designated A two proteins designated A and B a protein designated B a protein A and one-subunit a a protein designated A two proteins designated A and B a protein designated B ANSWER DOWNLOAD EXAMIANS APP
Enzymes The role of Asp 102 and His 57 during trypsin catalysis is to function as a proton shuttle clamp the substrate into the active site keep the specificity pocket open neutralize the charge on the other's side chain function as a proton shuttle clamp the substrate into the active site keep the specificity pocket open neutralize the charge on the other's side chain ANSWER DOWNLOAD EXAMIANS APP
Enzymes The cleavage specificity of trypsin and chymotrypsin depend in part on the size, shape, and charge of the active site or specificity pocket proximity of Ser 195 to the active site or specificity pocket absence of water in the active site presence of a low-barrier hydrogen bond in the active site or specificity pocket size, shape, and charge of the active site or specificity pocket proximity of Ser 195 to the active site or specificity pocket absence of water in the active site presence of a low-barrier hydrogen bond in the active site or specificity pocket ANSWER DOWNLOAD EXAMIANS APP
Enzymes The proteolysis rate enhancement by chymotrypsin (~1010 folds) corresponds to a reduction in activation energy of about 40 kJ/mol 58 kJ/mol 49 kJ/mol 88 kJ/mol 40 kJ/mol 58 kJ/mol 49 kJ/mol 88 kJ/mol ANSWER DOWNLOAD EXAMIANS APP
EXAMIANS