Show the complete reaction mechanism for the deamination of alanine until the amino group is transferred to the keto acid acceptor ⍺-ketoglutarate
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Show the complete reaction mechanism for the deamination of alanine until the amino group is transferred to the keto acid acceptor ⍺-ketoglutarate
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- Amino transferases catalyze the transfer of amino groups to alpha-keto acids with pyridoxal phosphate as the prosthetic group. Pyridoxal phosphate can accept an amino group, and its aminated form, pyridoxamine phosphate, can donate its amino group to an alpha-keto acid. Draw the detailed mechanism of the transamination reaction in the active site of an aminotransferase. Use the glutamate oxaloacetate transaminase as an example.Explain the chemical change that occurs in converting kynurenine (a product of tryptophan degradation) to kynurenate, a reaction in which α-ketoglutarate is transformed to glutamate.Amino transferases catalyze the transfer of amino groups to alpha-keto acids with pyridoxal phosphate as the prosthetic group. Pyridoxal phosphate can accept an amino group, and its aminated form, pyridoxamine phosphate, can donate its amino group to an alpha-keto acid. Illustrate the detailed mechanism of the transamination reaction in the active site of an aminotransferase. Use the glutamate oxaloacetate transaminase as an example.
- Lysine degradation requires removal of two amino groups. Removal of itsε-amino group gives a-aminoadipic semialdehyde. This product is thendegraded to acetoacetate by the same chemical strategy used to degrade thebranched-chain amino acids. Draw the proposed intermediates in this pathway (Hint: see Figure 18.14).The end products of tryptophan degradation are acetyl CoA and acetoacetyl CoA, yet tryptophan is a gluconeogenic amino acid in animals. Explain.What is the relationship of the optimal pH and temperature on the absorbance value of enzyme 6-O-α-rhamnosyl-D-glucosidase.
- Using the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.Thiolase is homologous in structure to the condensing enzyme. On the basis of this observation, propose a mechanism for the cleavage of 3-ketoacyl CoA by CoA.The sucrose substitute tagatose is produced by hydrolyzing lactose and then chemically converting one of the two resulting aldoses to a ketose. Which residue of lactose gives rise to tagatose?
- Consider the each of the amino acids in the peptide below. Ala-Ile-Asp-Arg-Gln-Gly-Pro-Gly-Ala-Tyr-Val-Ile-Gln-Leu If all of the amino acids are degraded to yield energy (ATP), explain how many Acetyl CoAs for oxidation to CO2 could be produced from this peptide. note: Do not make glucose at the beginning, however converting the TCA intermediates into molecules in the glycolytic pathway for optimal Acetyl CoA production is allowed. Be sure to show clearly which pathway will the Acetyl CoA enter (to yield ATP ultimately) under such conditionWhich of the following statements about the transamination and deamination steps of amino acid degradation is true? (A) a-ketoglutarate is always formed during a transamination between an amino acid and glutamate. (B) Transamination reactions produce glutamate that is deaminated after entering the urea cycle. (C) Free ammonia is removed from glutamate using glutamate dehydrogenase and NAD+ as an oxidizing agent. (D) The free NH4+ that is removed from glutamate during the deamination reaction is used to form glucose.(E) The carbon backbone that results from transamination enters the mitochondria to be used in the urea cycle.In the majority of cases, amino acid catabolism can be broken down into a two-stepprocess; ‘transamination’ followed by ‘oxidative deamination’. Serine doesn’t followthis two-step process; fully explain the reaction and mechanism involved in thedegradation process used to form its α-keto acid.