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What is it supposed to look like? the mechanism is a bit confusing to me
The structure of the active site of chymotrypsin is shown below. The catalytic triad shown (Ser...
The structure of the active site of chymotrypsin is shown below. The catalytic triad shown (Ser 195, His 57, and aspl02) are shown. A peptide with a phenylalanine is shown bound in the active site. 1. Chymotrypsin is a serine protease. The Km for chymotrypsin with N-acetylvaline ethyl ester is 8.8 X 102 M. The Km for the reaction with N-acetyltyrosine ethyl ester is 6.6 X 10 (a) Which substrate has the higher affinity for this enzyme? (b) Give a...
Picarate dehydrogenase (PDH) catalyzes the reduction of dextoacetate to picarate, while oxidizing NADH to NAD+. The...
Picarate dehydrogenase (PDH) catalyzes the reduction of
dextoacetate to picarate, while oxidizing NADH to NAD+.
The overall reaction and the active site of PDH is shown below. Use
curved arrow notation to propose a reasonable reaction mechanism
for this reaction.
НО, o НО 0 + NADH + H+ LOH + NAD+ picarate dehydrogenase 6/ 0 dextoacetate picarate C- NADH NH2 ZI H2C Arg171 CH2 + NH3 NH3 Arg 102 go dextoacetate CH2 HN HC His 195
dont know which ones. its a bit confusing when there are so many oxygens everywhere. someone...
dont know which ones. its a bit confusing when there are so
many oxygens everywhere. someone please help!!
7. (6 pts.) Sucralose is a sweetener found in many drinks and foods including yogurt. The structure of Sucralose is shown below. Circle all of the stereocenters in Sucralose. но c. HO но с ноYoo OHCl
what is the function of H57, S195, and water in each step for a serine protease. describe the movement of electrons show...
what is the function of H57, S195, and water in each
step for a serine protease. describe the movement of electrons
shown by the arrows in each step as well.
Mechanism Homework Consider the following mechanism for a serine protease: His-67 M-57 Ser-195 Asp-10 NY Ber-195 0 H-N. O HN, ROX HAHN His-57 Ser-195 OHN Ser-195 H-N Asp Asp-102 HAN "HAN HAHN EA His-57 Ser-195 H Ser105 Asp-102 H-N -N WHEN For each of the five steps determine: 1. The...
Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note...
Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note that some references may not break out each of these steps individually, but all steps should be ordered. There will be eight steps. First step His 57 catalyzes removal of H from Ser 195 hydroxyl. Ser 195's nucleophilic O attacks carbonyl C of substrate. The portion (the C-terminal end) of original substrate with the new amino terminus diffuses away. His 57 donates H to...
Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note...
Put these steps in the mechanism of chymotrypsin catalysis in
order from first to last. Note that your textbook may not break out
each of these steps individually, but all steps should be ordered.
(There will be eight steps.
)
first step last step Resulting OH attacks carbonyl of remaining substrate. His 57 donates H to Ser 195 O, leading to collapse of tetrahedral intermediate. mato Ser 195 the portion (N-terminal end) of original substrate with the new carboxylate terminus...
PIS) I Many protease enzymes have Cys-His-Asp catalytic triad. Draw the resting state of the active...
PIS) I Many protease enzymes have Cys-His-Asp catalytic triad. Draw the resting state of the active site of an enzyme with this kind of catalytic triad. Draw plausible tetrahedral intermediates (two structures needed) for hydrolysis of the peptide bond shown below. Ro-N^ RN
Number 2 is confusing a little bit. 1. (5 pts) Write the equilibrium constant K expression...
Number 2 is confusing a little bit.
1. (5 pts) Write the equilibrium constant K expression for the reaction below. C(s) + 2 H2 (9) = CH(9) Ke=[CH] [H₂] 2. (10 pts) In the reaction below, the reaction flask initially contained 0.50 M NO and 0.50 M Cl2. After the reaction reached equilibrium the concentration of NOCI was measured to be 0.25 M. What is the equilibrium constant Kc? Show all your work + 2 NOCI (9) 2 NOC49) 2...
5. Based on your understanding of the mechanism of proteases A. the figure below shows a part of the active sit...
5. Based on your understanding of the mechanism of proteases A. the figure below shows a part of the active site of the enzyme chymotrypsin. what are the identities of amino acids x and Y and what is this particular type of spatial arrangement of amino acids called? Alkoxide on X ? B. from the strucutres shown below, identify the two that represent the first and the second tetrahedral intermediates in the chymotrypsin catalyzed reaction. what type of attack and...
1. Give a sequence of reactions to accomplish the following transformation? Show mechanism 2. What reagent(s)...
1. Give a sequence of reactions to accomplish the following transformation? Show mechanism 2. What reagent(s) would accomplish the following? Show mechanism. R-CH2-NH2 R-C-NH2 3. What would result from the reactions shown below? Hsco-s-OCH3 large excess) NaOH нон H,0 но ОН "ОН (a and B) 4. Predict the major product of the following reaction. CHNNH 3 equivalents) но CHCH2OH Heat он CH2OH Draw the Haworth projection for chair conformation of a-D-Glucopyranose (shown below) CH2OH HO H OH OH
The structure of the active site of chymotrypsin is shown below. The catalytic triad shown (Ser 195, His 57, and aspl02) are shown. A peptide with a phenylalanine is shown bound in the active site. 1. Chymotrypsin is a serine protease. The Km for chymotrypsin with N-acetylvaline ethyl ester is 8.8 X 102 M. The Km for the reaction with N-acetyltyrosine ethyl ester is 6.6 X 10 (a) Which substrate has the higher affinity for this enzyme? (b) Give a...
Picarate dehydrogenase (PDH) catalyzes the reduction of
dextoacetate to picarate, while oxidizing NADH to NAD+.
The overall reaction and the active site of PDH is shown below. Use
curved arrow notation to propose a reasonable reaction mechanism
for this reaction.
НО, o НО 0 + NADH + H+ LOH + NAD+ picarate dehydrogenase 6/ 0 dextoacetate picarate C- NADH NH2 ZI H2C Arg171 CH2 + NH3 NH3 Arg 102 go dextoacetate CH2 HN HC His 195
dont know which ones. its a bit confusing when there are so
many oxygens everywhere. someone please help!!
7. (6 pts.) Sucralose is a sweetener found in many drinks and foods including yogurt. The structure of Sucralose is shown below. Circle all of the stereocenters in Sucralose. но c. HO но с ноYoo OHCl
what is the function of H57, S195, and water in each
step for a serine protease. describe the movement of electrons
shown by the arrows in each step as well.
Mechanism Homework Consider the following mechanism for a serine protease: His-67 M-57 Ser-195 Asp-10 NY Ber-195 0 H-N. O HN, ROX HAHN His-57 Ser-195 OHN Ser-195 H-N Asp Asp-102 HAN "HAN HAHN EA His-57 Ser-195 H Ser105 Asp-102 H-N -N WHEN For each of the five steps determine: 1. The...
Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note that some references may not break out each of these steps individually, but all steps should be ordered. There will be eight steps. First step His 57 catalyzes removal of H from Ser 195 hydroxyl. Ser 195's nucleophilic O attacks carbonyl C of substrate. The portion (the C-terminal end) of original substrate with the new amino terminus diffuses away. His 57 donates H to...
Put these steps in the mechanism of chymotrypsin catalysis in
order from first to last. Note that your textbook may not break out
each of these steps individually, but all steps should be ordered.
(There will be eight steps.
)
first step last step Resulting OH attacks carbonyl of remaining substrate. His 57 donates H to Ser 195 O, leading to collapse of tetrahedral intermediate. mato Ser 195 the portion (N-terminal end) of original substrate with the new carboxylate terminus...
PIS) I Many protease enzymes have Cys-His-Asp catalytic triad. Draw the resting state of the active site of an enzyme with this kind of catalytic triad. Draw plausible tetrahedral intermediates (two structures needed) for hydrolysis of the peptide bond shown below. Ro-N^ RN
Number 2 is confusing a little bit.
1. (5 pts) Write the equilibrium constant K expression for the reaction below. C(s) + 2 H2 (9) = CH(9) Ke=[CH] [H₂] 2. (10 pts) In the reaction below, the reaction flask initially contained 0.50 M NO and 0.50 M Cl2. After the reaction reached equilibrium the concentration of NOCI was measured to be 0.25 M. What is the equilibrium constant Kc? Show all your work + 2 NOCI (9) 2 NOC49) 2...
5. Based on your understanding of the mechanism of proteases A. the figure below shows a part of the active site of the enzyme chymotrypsin. what are the identities of amino acids x and Y and what is this particular type of spatial arrangement of amino acids called? Alkoxide on X ? B. from the strucutres shown below, identify the two that represent the first and the second tetrahedral intermediates in the chymotrypsin catalyzed reaction. what type of attack and...
1. Give a sequence of reactions to accomplish the following transformation? Show mechanism 2. What reagent(s) would accomplish the following? Show mechanism. R-CH2-NH2 R-C-NH2 3. What would result from the reactions shown below? Hsco-s-OCH3 large excess) NaOH нон H,0 но ОН "ОН (a and B) 4. Predict the major product of the following reaction. CHNNH 3 equivalents) но CHCH2OH Heat он CH2OH Draw the Haworth projection for chair conformation of a-D-Glucopyranose (shown below) CH2OH HO H OH OH
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