Homework Answers
7a. In the diagram there is an aromatic ring next to W44, so we can tell W44 helps in hydrphobic interaction.
7b. D19 is an acid group that acts as nucleophile. It attacks on electrophilic center on substrates that fit in the cavity.
7c. H57 acts as a proton donor. Histidine acts as catalytic element. It donates and takes back hydrogen as needed.
7d. According to mechanism it is acid catalysed nucleophilic attack.
7e. Yes, it goes through an intermediate.
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7. Using the active site shown below answer the following questions: The amino acids in the...
Which statement about enzyme catalysis is false? All of the active site amino acids are next...
Which statement about enzyme catalysis is false? All of the active site amino acids are next to each other in the primary sequence. Enzymes speed up reactions by forming specific non-covalent bonds between the enzyme amino acids and the transition state molecule. Some enzymes require other molecules, called cofactors, to carry out chemical reactions. Generally, the most important amino acids for an enzyme's function are those in the active site. Question 6 1 pt When [S] is much more than...
2. The reaction below is catalyzed by the CK enzyme: NH O | NHA | СК...
2. The reaction below is catalyzed by the CK enzyme: NH O | NHA | СК O= H₂N Ņ coo eo T N con + ATP + ADP Below is a picture of the active site for this enzyme. The red atoms are the amino acids in the CK protein. The blue structure is the substrate, the orange is the phosphate end of ATP. All dashed lines are showing interactions and the curved arrows are showing the mechanism. The wavy...
2. The reaction below is catalyzed by the CK enzyme: NH2 OP H2N H₂N N Ń...
2. The reaction below is catalyzed by the CK enzyme: NH2 OP H2N H₂N N Ń cooK COO - INN CO + ATP + ADP Below is a picture of the active site for this enzyme. The red atoms are the amino acids in the CK protein. The blue structure is the substrate, the orange is the phosphate end of ATP. All dashed lines are showing interactions and the curved arrows are showing the mechanism. The wavy lines indicate that...
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...
The second part of the mechanism for histidyl-tRNA-synthetase is shown below. Active site residues are in...
The second part of the mechanism for histidyl-tRNA-synthetase is shown below. Active site residues are in black and the substrates are shown in green. Examine the image and complete the following questions. RNAH A76 Arg113 Gin 127 Glu131 M-o Histidy-Adenylate Arg259 Tyr264 c 1. Describe the role of Arg259 in the active site of histidyl- RNA-synthetase. Proton anor acid 2. If the substrates for this enzyme are histidine, ATP, and tRNAHs. Describe overall (not mechanism steps) what must have happened...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and ...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
The following questions are based on the papin mechanism below: Explain the role of each amino acid in the catalytic triad. Site directed mutagenesis replacing the active site asp in the papain protea...
The
following questions are based on the papin mechanism below:
Explain the role of each amino acid in the catalytic triad.
Site directed mutagenesis replacing the active site asp in the
papain protease with an ala showed that catalytic activity was not
significantly affected. Why would you think that asp is not so
critical in the cysteine proteases?
Hi R CH2 NH-R oe 0 hole oxyanion hole 0 oxyanion hole CH a)
Hi R CH2 NH-R oe 0 hole oxyanion...
Biochemistry. Please answer all completely. 13. Identify the electrophilic center and nucleophile in the below image...
Biochemistry. Please answer all completely.
13. Identify the electrophilic center and nucleophile in the below image : R 14. Give an example of amino acids with R group shown below which can function as nucleophile during enzyme catalysis. Nucleophiles Negatively charged oxygen (as in an unprotonated hydroxyl group or an ionized carboxylic acid) Negatively charged sulfhydryl Uncharged amine group HN Imidazole 15. Identify the amino acids with the following side chains and also define if they will work as acid...
biochemistry if you could please help me answer the following questions! 741) (5 pts) Transition state theory relate...
biochemistry
if you could please help me answer the following questions!
741) (5 pts) Transition state theory relates the rate constant to the free energy of activation, AG. How can enzymes reduce the activation energy barrier? a) decrease the free energy of the product b) high affinity binding to the transition state c) increase the free energy of the substrate d) increase entropy upon release of product e) bind to the substrate with high affinity 2) (5 pts) Which is...
5. Made up amino acids Bleucine and Isobleucine are synthesized in a series of steps from...
5. Made up amino acids Bleucine and Isobleucine are synthesized in a series of steps from made up sugar Blorptose. These are essential for the organism to grow but can be supplied in the medium otherwise to complement the growth defect of mutants when amino acids cannot be synthesized. There are a number of chemical intermediates that are each synthesized by enzymes. Some enzymes in the pathway give both Bleu' and Isobleu phenotypes, while others are only Bleu' or Isableu....
Which statement about enzyme catalysis is false? All of the active site amino acids are next to each other in the primary sequence. Enzymes speed up reactions by forming specific non-covalent bonds between the enzyme amino acids and the transition state molecule. Some enzymes require other molecules, called cofactors, to carry out chemical reactions. Generally, the most important amino acids for an enzyme's function are those in the active site. Question 6 1 pt When [S] is much more than...
2. The reaction below is catalyzed by the CK enzyme: NH O | NHA | СК O= H₂N Ņ coo eo T N con + ATP + ADP Below is a picture of the active site for this enzyme. The red atoms are the amino acids in the CK protein. The blue structure is the substrate, the orange is the phosphate end of ATP. All dashed lines are showing interactions and the curved arrows are showing the mechanism. The wavy...
2. The reaction below is catalyzed by the CK enzyme: NH2 OP H2N H₂N N Ń cooK COO - INN CO + ATP + ADP Below is a picture of the active site for this enzyme. The red atoms are the amino acids in the CK protein. The blue structure is the substrate, the orange is the phosphate end of ATP. All dashed lines are showing interactions and the curved arrows are showing the mechanism. The wavy lines indicate that...
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...
The second part of the mechanism for histidyl-tRNA-synthetase is shown below. Active site residues are in black and the substrates are shown in green. Examine the image and complete the following questions. RNAH A76 Arg113 Gin 127 Glu131 M-o Histidy-Adenylate Arg259 Tyr264 c 1. Describe the role of Arg259 in the active site of histidyl- RNA-synthetase. Proton anor acid 2. If the substrates for this enzyme are histidine, ATP, and tRNAHs. Describe overall (not mechanism steps) what must have happened...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
The
following questions are based on the papin mechanism below:
Explain the role of each amino acid in the catalytic triad.
Site directed mutagenesis replacing the active site asp in the
papain protease with an ala showed that catalytic activity was not
significantly affected. Why would you think that asp is not so
critical in the cysteine proteases?
Hi R CH2 NH-R oe 0 hole oxyanion hole 0 oxyanion hole CH a)
Hi R CH2 NH-R oe 0 hole oxyanion...
Biochemistry. Please answer all completely.
13. Identify the electrophilic center and nucleophile in the below image : R 14. Give an example of amino acids with R group shown below which can function as nucleophile during enzyme catalysis. Nucleophiles Negatively charged oxygen (as in an unprotonated hydroxyl group or an ionized carboxylic acid) Negatively charged sulfhydryl Uncharged amine group HN Imidazole 15. Identify the amino acids with the following side chains and also define if they will work as acid...
biochemistry
if you could please help me answer the following questions!
741) (5 pts) Transition state theory relates the rate constant to the free energy of activation, AG. How can enzymes reduce the activation energy barrier? a) decrease the free energy of the product b) high affinity binding to the transition state c) increase the free energy of the substrate d) increase entropy upon release of product e) bind to the substrate with high affinity 2) (5 pts) Which is...
5. Made up amino acids Bleucine and Isobleucine are synthesized in a series of steps from made up sugar Blorptose. These are essential for the organism to grow but can be supplied in the medium otherwise to complement the growth defect of mutants when amino acids cannot be synthesized. There are a number of chemical intermediates that are each synthesized by enzymes. Some enzymes in the pathway give both Bleu' and Isobleu phenotypes, while others are only Bleu' or Isableu....
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