Enzymes Tryprotophan synthetase of E.coli, a typical bifunctional oligomeric enzyme consist of a protein designated A a protein A and one-subunit a a protein designated B two proteins designated A and B a protein designated A a protein A and one-subunit a a protein designated B two proteins designated A and B 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 size, shape, and charge of the active site or specificity pocket 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 absence of water in the active site size, shape, and charge of the active site or specificity pocket 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 88 kJ/mol 49 kJ/mol 40 kJ/mol 58 kJ/mol 88 kJ/mol 49 kJ/mol 40 kJ/mol 58 kJ/mol ANSWER DOWNLOAD EXAMIANS APP
Enzymes The nucleophile in serine proteases is both (a) and (b) Serine Asparagine water both (a) and (b) Serine Asparagine water ANSWER DOWNLOAD EXAMIANS APP
Enzymes What is the specificity of the Clostripain protease? None of these It cleave after Arg residues It cleave after Lys residues It cleave after His residues None of these It cleave after Arg residues It cleave after Lys residues It cleave after His residues ANSWER DOWNLOAD EXAMIANS APP
Enzymes The role of Asp 102 and His 57 during trypsin catalysis is to 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 clamp the substrate into the active site neutralize the charge on the other's side chain ANSWER DOWNLOAD EXAMIANS APP
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