Using the figure below, determine the metabolic intermediate(s) directly produced from the carbon atoms of each of the following amino acids. Check all thatapply for each part.alanine, cysteine,isoleucine, leucine,Part 1 of 2Valineleucine, lysine,glycine, serine,pyruvatethreonine, tryptophanthreonine, tryptophanphenylalanine,tryptophan, tyrosineacetyl CoA acetoacetyl CoA(CH,COCH,COSCA)asparagine,aspartic acidoxaloacetatecitratemalateisocitrateCitric acidcyclephenylalanine,tyrosinefumaratePart 2 of 2Asparaginefumarateacetoacetyl CoApyruvateoxaloacetatesuccinyl CoAa-ketoglutarateacetyl CoANone of the abovefumarateacetoacetyl CoApyruvateoxaloacetatesuccinyl CoAa-ketoglutarateacetyl CoANone of the abovea-ketoglutaratearginine, glutamic acid,glutamine, histidine,prolineKsuccinatesuccinyl CoAisoleucine, methionine,threonine, valine

Part 1:The metabolic intermediate directly produced from the carbon atoms of valine is…

Answered: Using the figure below, determine the…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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ẞ-Calendic acid is an omega-6, conjugated fatty acid that is the all-trans isomer of a-calendic acid. HOOC—CH,CH, CH, CH,CH, CH, Part: 0/2 Part 1 of 2 H C=C H C-H H-C H C=C H CH₂ -CH2-CH2-CH2-CH₂ When this fatty acid is partially hydrogenated with one equivalent of H₂ in the presence of a Pd catalyst, a mixture of constitutional isomers is formed. Modify the given structure to draw one of these possible products.
Draw the reactions that convert fructose into glycolyticintermediates.
Classify the following amino acids base on their side chain if it's either -Non-polar aliphatic R group -Aromatic R groups -Polar uncharged R groups -Positively charged R groups -Polar, uncharged R groups -Negatively charged R groups
Explain the difference between essential and nonessential amino acids. How many of each are there? Identify and describe two essential and two nonessential amino acids. What does the term "conditionally essential" mean? Give an example.
Determine the amino acid sequence of Peptide A, which was obtained by hydrolyzing a larger peptide with trypsin, using the data below: Total hydrolysis of Peptide A produces (Ala2, Arg, Glu, Gly, Met, Pro2, Ser, Tyr). Sequential Edman degradation of Peptide A produces a derivative of Ala in the first cycle; a derivative of Serine in the second cycle; and a derivative of Proline in the third cycle. Cleavage of Peptide A with chymotrypsin yields two peptides: a tripeptide III containing Ala, Arg and Gly; and a heptapeptide IV containing Ala, Glu, Met, Pro2, Ser and Tyr. Edman treatment of tripeptide III generated a derivative of Alanine. Cleavage of Peptide A with cyanogen bromide (which cleaves peptides on the C-terminal side of Methionine) yields two pentapeptides labeled I and II. Total hydrolysis or peptide I indicate that it contains Ala, Arg, Gly, Pro and Tyr; pentapeptide II contains Ala, Glu, Met, Pro, and Ser.
For the determination of fatty acid composition, transesterification is done in a warm aqueous solution ofa) KCl+methanolb) KOH+methanolc) NaOH+methanold) H2O+methanol
Which of the following amino acids would you expect to find more often near the center of a folded globular protein? Which ones would you expect to find more often exposed to the outside? explain your answers. Ser, Ser-p (a Ser residue that is phosphorylated), Leu, Lys, Gln, His, Phe, Val, Ile, Met, Cys–S–S–Cys (two cysteines that are disulfide- bonded), and Glu. Where would you expect to find the most N-terminal amino acid and the most C-terminal amino acid?
Many enzymes are switched "on" by attachment of a phosphate group at a specific serine somewhere on the protein (phosphorylation). The basic reaction is: E + ATP2 Ep + ADP Po SERINE PHOSPHO SERINC (Note the "squiggles" before the backone amide and carbonyl indicate the polypeptide chain continues on either side of the serine). For phosphorylation to have this effect, there has to be some equilibrium between inactive and active forms conformations of the enzyme: [Eactive] [Einactive] Einactive 2 Eactive; K* The same basic equilibrium must exist for the phosphorylated protein: [Ep,active] [Ep,inactive] EP,inactive 2 Ep,active; Kp = (a) If phosphorylation increases the measured activity of the enzyme, is K* or K larger? Why? (b) Does the phosphorylation site need to be near the site where the enzyme binds its substrate (e.g. the reactant whose chemistry it catalyzes)? Why or why not?
Compare and contrast lactose intolerance with galactosemia.(Hint: Make a table.)
Please calculate the number of ATP that can be generated from one molecule of the fatty acid shown below. (Please "explain" your calculation step-by-step) ОНННННННН Н Н Н ПТТТТТТТТТТI но-с-с-с-с-с-с-с-с-с-с-с-с-н | | | | | | | | |.. ННННННННН Н Н
Which of the following statements about sugar polymers and glycosaminoglycans is/are true? Glucosamine, an amino sugar, would be positively charged physiologically unless it is part of an amide bond. Chitin is a homopolymer of GlcNac in beta 1--> 4 linkages. Amylose is a homopolymer of glucose containing alpha 1--> 6 linkages. Amylopectin in a non-reducing sugar polymer consisting solely of glucose monomers. Agarose is a highly charged sugar polymer used in electrophoresis. A core of hyaluronan protein is linked to an aggrecan polysaccharide in the extracellular matrix around joints and tendons. Mucins are secreted proteins that contain branched oligosaccharides linked to serine residues. None of the options shown is true. The glycosaminoglycan "hyaluronic acid" would carry more negative charge overall when compared to a polymer of "chondroitin" of the same length. Please answer very soon will give rating surely Complete Answer needed
Briefly discuss the synthesis of selenocysteine amino acid.

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