Enzymes Tryprotophan synthetase of E.coli, a typical bifunctional oligomeric enzyme consist of 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 a protein A and one-subunit a ANSWER DOWNLOAD EXAMIANS APP
Enzymes Common feature in all serine proteases is a hydrophilic specificity pocket single reactive serine residue hydrophobic specificity pocket cluster of reactive serine residues hydrophilic specificity pocket single reactive serine residue hydrophobic specificity pocket cluster of reactive serine residues ANSWER DOWNLOAD EXAMIANS APP
Enzymes The nucleophile in serine proteases is water Asparagine Serine both (a) and (b) water Asparagine Serine both (a) and (b) ANSWER DOWNLOAD EXAMIANS APP
Enzymes Before they can react, many molecules need to be destabilized. This state is typically achieved through the input of a small amount of activation energy oxidizing the molecules by removing electrons changing the three-dimensional shape of the molecule changing the reaction from a biosynthetic to a catabolic pathway the input of a small amount of activation energy oxidizing the molecules by removing electrons changing the three-dimensional shape of the molecule changing the reaction from a biosynthetic to a catabolic pathway ANSWER DOWNLOAD EXAMIANS APP
Enzymes The cleavage specificity of trypsin and chymotrypsin depend in part on the 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 size, shape, and charge of 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 88 kJ/mol 40 kJ/mol 49 kJ/mol 58 kJ/mol 88 kJ/mol 40 kJ/mol 49 kJ/mol 58 kJ/mol ANSWER DOWNLOAD EXAMIANS APP
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