Enzymes The E.coli pyruvic acid dehydrogenase complex is reported to Catalyze the oxidation of pyruvic acid to acetyl Co A and CO2 Catalyze the reduction of pyruvic acid to acetyl Co A and CO2 retard 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 Catalyze the reduction of pyruvic acid to acetyl Co A and CO2 retard the reduction of pyruvic acid to acetyl Co A and CO2 decatalyze the oxidation of pyruvic acid to acetyl Co A and CO2 ANSWER DOWNLOAD EXAMIANS APP
Enzymes The proteolysis rate enhancement by chymotrypsin (~1010 folds) corresponds to a reduction in activation energy of about 49 kJ/mol 88 kJ/mol 40 kJ/mol 58 kJ/mol 49 kJ/mol 88 kJ/mol 40 kJ/mol 58 kJ/mol ANSWER DOWNLOAD EXAMIANS APP
Enzymes Which of the following (s) is/are serine proteases? all of these Trypsin Chymotrypsin Elastase all of these Trypsin Chymotrypsin Elastase ANSWER DOWNLOAD EXAMIANS APP
Enzymes Which of the following is false statement with regard to comparison between Serine and HIV proteases? Both show specificity for certain amino acid sequences Both use nucleophilic attack to hydrolyze the peptide bond Both require water to complete the catalytic cycle Both forms an acyl-enzyme intermediate Both show specificity for certain amino acid sequences Both use nucleophilic attack to hydrolyze the peptide bond Both require water to complete the catalytic cycle Both forms an acyl-enzyme intermediate ANSWER DOWNLOAD EXAMIANS APP
Enzymes Common feature in all serine proteases is a hydrophilic specificity pocket single reactive serine residue cluster of reactive serine residues hydrophobic specificity pocket hydrophilic specificity pocket single reactive serine residue cluster of reactive serine residues hydrophobic specificity pocket ANSWER DOWNLOAD EXAMIANS APP
Enzymes The nucleophile in serine proteases is both (a) and (b) Serine water Asparagine both (a) and (b) Serine water Asparagine ANSWER DOWNLOAD EXAMIANS APP
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