draw the mechanism for the enzyme aspartate aminotransferase
draw the mechanism for the enzyme aspartate aminotransferase
Homework Answers
Mechanism
is given in the attached images.
Nursing Skill/Concept: Laboratory Test Procedure Name: Aspartate Aminotransferase (AST) Name: Date: Indications (Symptoms Pl. may be...
Nursing Skill/Concept: Laboratory Test Procedure Name: Aspartate Aminotransferase (AST) Name: Date: Indications (Symptoms Pl. may be displaying) Nursing Interventions Potential Complications Outcomes/Evaluations Patient Education
3. Draw an the mechanism showing how the glutamine-PRPP amidotransferase adds biosynthesis. 4. Aspartate is highly...
3. Draw an the mechanism showing how the glutamine-PRPP
amidotransferase adds biosynthesis. 4. Aspartate is highly involved
in the biosynthesis of purines and pyrimidines. Show the two steps
where aspartate-derived nitrogen is added in the synthetic pathway
leading to adenosine 5-monophosphate (AMP) 5. Show the steps where
asparatate-derived nitrogen is added in the synthesis cytosine
5-monophosphate (CMP)
3. Draw an the mechanism showing how the glutamine-PRPP amidotransferase adds biosynthesis. 4. Aspartate is highly involved in the biosynthesis of purines and...
Imagine that you have discovered an enzyme that catalyzes synthesis of asparagine from aspartate and NH3....
Imagine that you have discovered an enzyme that catalyzes synthesis of asparagine from aspartate and NH3. The reaction requires ATP. What do you postulate is the “activated” intermediate ? (Draw it and name it)
Use your knowledge of generic amino acid aminotransferase mechanism to push the arrows for the complete...
Use your knowledge of generic amino acid aminotransferase mechanism to push the arrows for the complete alanine aminotransferase reaction. The alpha-keto acid used is pyruvate; use a generic amino acid.
5. A protonated histidine residue in the active site of aspartate transcarbamoylase, ATCase, is thought to...
5. A protonated histidine residue in the active site of aspartate transcarbamoylase, ATCase, is thought to be important in stabilizing the transition state of the bound substrate. a) Sketch a graph showing the pH dependence of the catalytic rate, assuming that this interaction is essential and dominates the pH-activity profile of the enzyme. Provide the biochemical basis for your graph. b) Identify one of the two substrates involved in the reaction catalyzed by ATCase and the enzyme class for ATCase....
Draw an arrow mechanism to show the reaction. Based on the illustrated stereochemistry, does the enzyme...
Draw an arrow mechanism to show the reaction. Based on the
illustrated stereochemistry, does the enzyme direct the Br cation
to the top or bottom face of the alkene as drawn?
Prelaureatin, a marine natural product, is thought to be biosynthesized from laurediol by the following enzyme catalyzed reaction: "Br+" H -=
2. Draw out both steps of the malic enzyme mechanism for the conversion of malate to...
2. Draw out both steps of the malic enzyme mechanism for the conversion of malate to pyruvate. Include nicotinamide moieties, acid/base catalysis, and electron movement
Draw two aspartate side chains and how they hydrogen bond to eachother
Draw two aspartate side chains and how they hydrogen bond to eachother
15. Compare the catalytic activity of of the following enzymes: carbonic anhydrase, aspartate transcarbomylase (ATcase), restriction...
15. Compare the catalytic activity of of the following enzymes: carbonic anhydrase, aspartate transcarbomylase (ATcase), restriction enzymes and myosins. (40 points) What is unique about each active site with regards to types of amino acid residues a) located in active site and interaction with substrate? b) Briefly what is the mechanism of catalysis in each active site? Are cofactors or coenzymes required by the enzymes and if so what is the role of the cofactor/coenzyme in catalysis? c) How is...
2. (12 points) Draw the mechanism for triose phosphate isomerase using arrow pushing. The enzyme contains...
2. (12 points) Draw the mechanism for triose phosphate isomerase using arrow pushing. The enzyme contains two key active site amino acid residues, Glu and His, seen below. Glu His -OH OPO, OPO,
Nursing Skill/Concept: Laboratory Test Procedure Name: Aspartate Aminotransferase (AST) Name: Date: Indications (Symptoms Pl. may be displaying) Nursing Interventions Potential Complications Outcomes/Evaluations Patient Education
3. Draw an the mechanism showing how the glutamine-PRPP
amidotransferase adds biosynthesis. 4. Aspartate is highly involved
in the biosynthesis of purines and pyrimidines. Show the two steps
where aspartate-derived nitrogen is added in the synthetic pathway
leading to adenosine 5-monophosphate (AMP) 5. Show the steps where
asparatate-derived nitrogen is added in the synthesis cytosine
5-monophosphate (CMP)
3. Draw an the mechanism showing how the glutamine-PRPP amidotransferase adds biosynthesis. 4. Aspartate is highly involved in the biosynthesis of purines and...
5. A protonated histidine residue in the active site of aspartate transcarbamoylase, ATCase, is thought to be important in stabilizing the transition state of the bound substrate. a) Sketch a graph showing the pH dependence of the catalytic rate, assuming that this interaction is essential and dominates the pH-activity profile of the enzyme. Provide the biochemical basis for your graph. b) Identify one of the two substrates involved in the reaction catalyzed by ATCase and the enzyme class for ATCase....
Draw an arrow mechanism to show the reaction. Based on the
illustrated stereochemistry, does the enzyme direct the Br cation
to the top or bottom face of the alkene as drawn?
Prelaureatin, a marine natural product, is thought to be biosynthesized from laurediol by the following enzyme catalyzed reaction: "Br+" H -=
2. Draw out both steps of the malic enzyme mechanism for the conversion of malate to pyruvate. Include nicotinamide moieties, acid/base catalysis, and electron movement
15. Compare the catalytic activity of of the following enzymes: carbonic anhydrase, aspartate transcarbomylase (ATcase), restriction enzymes and myosins. (40 points) What is unique about each active site with regards to types of amino acid residues a) located in active site and interaction with substrate? b) Briefly what is the mechanism of catalysis in each active site? Are cofactors or coenzymes required by the enzymes and if so what is the role of the cofactor/coenzyme in catalysis? c) How is...
2. (12 points) Draw the mechanism for triose phosphate isomerase using arrow pushing. The enzyme contains two key active site amino acid residues, Glu and His, seen below. Glu His -OH OPO, OPO,
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