Enzymes The E.coli pyruvic acid dehydrogenase complex is reported to Catalyze the reduction of pyruvic acid to acetyl Co A and CO2 decatalyze the oxidation of pyruvic acid to acetyl Co A and CO2 Catalyze the oxidation of pyruvic acid to acetyl Co A and CO2 retard the reduction of pyruvic acid to acetyl Co A and CO2 Catalyze the reduction of pyruvic acid to acetyl Co A and CO2 decatalyze the oxidation of pyruvic acid to acetyl Co A and CO2 Catalyze the oxidation of pyruvic acid to acetyl Co A and CO2 retard the reduction of pyruvic acid to acetyl Co A and CO2 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, C, and D will all still be produced A and B will still be produced, but not C or D A will still be produced, but not B, C, or D A, B, and C will still be produced, but not D A, B, C, and D will all still be produced A and B will still be produced, but not C or D A will still be produced, but not B, C, or D A, B, and C will still be produced, but not D ANSWER DOWNLOAD EXAMIANS APP
Enzymes Enzyme-driven metabolic pathways can be made more efficient by All of these fixing enzymes into membranes so that they are adjacent to each other grouping enzymes into free-floating, multienzyme complexes concentrating enzymes within specific cellular compartments All of these fixing enzymes into membranes so that they are adjacent to each other grouping enzymes into free-floating, multienzyme complexes concentrating enzymes within specific cellular compartments ANSWER DOWNLOAD EXAMIANS APP
Enzymes Tryprotophan synthetase of E.coli, a typical bifunctional oligomeric enzyme consist of a protein designated A a protein designated B two proteins designated A and B a protein A and one-subunit a a protein designated A a protein designated B two proteins designated A and B a protein A and one-subunit a ANSWER DOWNLOAD EXAMIANS APP
Enzymes The cleavage specificity of trypsin and chymotrypsin depend in part on the absence of water in the active site presence of a low-barrier hydrogen bond in the active site or specificity pocket proximity of Ser 195 to the active site or specificity pocket size, shape, and charge of 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 proximity of Ser 195 to the active site or specificity pocket size, shape, and charge of the active site or specificity pocket ANSWER DOWNLOAD EXAMIANS APP
Enzymes The role of Asp 102 and His 57 during trypsin catalysis is to clamp the substrate into the active site neutralize the charge on the other's side chain keep the specificity pocket open function as a proton shuttle clamp the substrate into the active site neutralize the charge on the other's side chain keep the specificity pocket open function as a proton shuttle ANSWER DOWNLOAD EXAMIANS APP
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