what would happen to the flow of carbon in central metabolism if alpha-ketoglutarate was being removed to make the amino acid glutamate?
The flow of carbon would reduce if the alpha ketogluterate in the cell was made into the amino acid glutamate. Since alpha ketogluterate is a critical part of the TCA cycle and the TCA cycle is a vital part of respiration, the flow of carbon and energy would reduce.
The TCA cycle would not go on in the absence of alpha ketogluterate. anaplerotic reactions will also not occur in the absence of alpha ketogluterate.
what would happen to the flow of carbon in central metabolism if alpha-ketoglutarate was being removed...
Describe what happens in glutamate metabolism. How does this amino acid work into central metabolism for carbon and energy?
alpha-Ketoglutarate plays a central role in the biosynthesis of several amino acids. Write a sequence of enzymatic reactions that could results in the NET synthesis of alpha-ketoglutarate from pyruvate. You may use other cofactors as required (e.g. NADH, ATP). There is no need to show structures, but indicate the name of each intermediate, the name of the enzyme, and balance each reaction for cosubstrates and cofactors. Each of the carbons in your alpha-ketoglutarate product must have originated from pyruvate.
Select all that apply. What amino acids are synthesized from alpha - ketoglutarate? histidine valine glutamate methionine proline arginine isoleucine alanine lysine glutamine phenylalanine leucine
What are the resulting products of transamination between glutamate and oxaloacetate, respectively? Select one: a. alpha-ketoglutarate and aspartate b. alpha-ketoglutarate and alanine c. glutamine and aspartate d. glutamate and alanine e. None of these
What would happen in the synthesis of sulfanilamide if the amino group were not protected as an amide in the chlorosulfonation step? If the Amino group were NOT protected, it would do a ____ substitution on chlorosulfonic acid. Later in the sequence, this group ____ be removed without cleaving the other sulfonamide group. electrophilic; could not nucleophilic; could not nucleophilic; could electrophilic; could
Question 6 2 pts Some amino acids can supply the carbon required for gluconeogenesis by undergoing a reaction catalyzed by an aminotransferase, an enzyme that interconverts amino acids and -keto acids. Aspartate aminotransferase catalyzes the reaction shown below. aspartate + a-ketoglutarate - oxalacetate + glutamate A biochemist studying metabolism feeds 4-[14C]-aspartate (asparatate that has 14C, the radioactive isotope of carbon, at the sidechain carboxylate) to his rats. After sacrificing the rats he is unable to find any +4C in glucose....
What is the inborn error of metabolism? Why we are suggested to know about the basic science of the unborn error of metabolism before we are starting the section of B-vitamins in amino acid and one-carbon metabolism?
3. Briefly describe the importance of accurate splicing. What happens if too much RNA is removed during splicing? What happens if not enough RNA is removed during splicing? What would happen if a splicing event results in the deletion of a single nucleotide from the beginning of an exon? (4 points) 3. Briefly describe the importance of accurate splicing. What happens if too much RNA is removed during splicing? What happens if not enough RNA is removed during splicing? What...
12. If an aminoacyl-tRNA synthetase attaches the wrong amino acid to a tRNA, what will happen? O The tRNA won't fold into the correct secondary structure. O The tRNA will be rejected by the ribosome. O The wrong amino acid will be added to the polypeptide, but it will be removed during proofreading. O The wrong amino acid will be added to the polypeptide.
If the mutation is in isocitrate dehydrogenase, what would you expect to happen to the levels of : (increase/decrease) isocitrate a- ketoglutarate glyoxylate