For the enzymatically catalyzed reactions shown below, classify the enzymes as oxidoreductases transferases, hydrolases, lyases, isomerases,...
There are 6 classes of enzymes: oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases. Decide to which class each of the enzymes belongs. 3. 1) Papain Ha R3 O R3 Papain 2) Aspartase NH? +NH3 OOC H Aspartase 3) Coo lactate dehydrogenase ??? ?? Lactate dehydrogenase
What is the name of the class of enzymes that would catalyze each of the following reactions? (a) hydrolysis of sucrose O hydrolase isomerase lyase oxidoreductase transferase (b) moving an amino group from one molecule to another hydrolase somerase lyase oxidoreductase transferase (c) addition of oxygen hydrolase isomerase lyase oxidoreductase transferase (d) removing hydrogen atoms hydrolasee isomerase lyase oxidoreductasee transferase
OH OHC Use the following choices to classify the enzymatic reaction shown In questions 8 A) a transferase B) a lyase C) an Isomerase D) a hydrolase E) a ligase AB) an oxidoreductase (bubble both letters for this answer) 18-22 но enayme ATP+ он OH ADP 18. + NADH+H HO 19. 0 enzyme 20. CHOPOS o3POCH2 CH2OPOs enzyme 2O3POCH2 HO H HO OH он oPOS 21. enzyme coo OPO3 HO coo 22. OH OHC Use the following choices to classify...
There are two sets of reactions in glycolysis in which phosphate intermediates are synthesized in the first reaction and their energy harvested as ATP in the second reaction. Part A Identify the two sets of reactions. Check all that apply. O Step 1. Phosphorylation Step 2. Isomenzation Step 3. Phosphorylation Step 4. Cleavage Step 5, Isomerization Step 6, Oxidation and Phosphorylaton Step 7. Phosphate Transfer Step 8. Isomerization Step 9, Dehydration C) □ a Step 10. Phosphate Transfer We were...
14. Classify the following reactions as oxidoreductase, transferase, hydrolase, lyake, isomerase, or ligase. o-Reduction equivalent ty Crtr Case Bred Ared Ao Box 8-C AB A Oxidoecacte 8 A- 8-OH A-H Ho hyclrolcgk Iso A XDP x-AG.UC \৩০১০ A XTP A-B 15. List the catalytic triad in the active site of chymotrypsin. S Asa r
First question: Which type of enzyme fron table 11-2 catalyzes the following reactions (a) 600 c=0 CH + NADH + H - 500- + NAD HO-- CH, COO H-CH(CH HỘI NH ADP + P 5. On the free energy diagram shown, label the intermediate(s) and transition state(s). Is the reaction thermodynamically favorable? 6. Urcase, the first enzyme to be crystallized, is inhibited in the presence of Hg, Cd, or Co ions What does this information suggest about the catalytic mechanism...
the conversion of L-Threonine to L-isoleucine occurs in a series of 5 enzymatically catalyzed steps shown below. isoleucine is a noncompetitive inhibitor of one of these enzymes. which is the one that is most effectively inhibited by Ile? The conversion of L-Threonine to L-Isoleucine occurs in a series of 5 enzymatically catalyzed steps shown below. Isoleucine is a noncompetitive inhibitor of one of these enzymes. Which is the one that is most effectively inhibited by Ile? E1 E2 E3 E4...
1. You are considering the following biological reactions that are catalyzed by specific enzymes as shown below. In reaction #1, enzyme El catalyzes the conversion of compound A to compound B in a truly reversible reaction in which the reverse reaction is just as likely as the forward reaction. In reaction #3, enzyme E2 catalyzes an energy requiring reaction that uses compounds C and D as substrates to produce compound E. In reaction #3, enzyme E3 catalyzes an energy producing...
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much of their three dimensional shape is the result of interactions between the R (variable) groups of their amino acids. The active site is the portion of the enzyme that will interact with the substrate the molecule that the enzyme acts upon. The nature and arrangement of amino acids in the active site make each enzyme specific to a substrate and to the reaction it...