Failure of anti-oxidant function results in the hydroxylation of an aromatic acid of Enzyme Z andits activation, so that it degrades protoporphyrin to porphyrin, an unstable product. When hit bylight, this product further degrades to form a compound responsible for the lesions andexcruciating pain the man suffers. The mutation also affected an amino acid at the N-terminal ofEnzyme X. Sequencing of the first seven (7) amino acids at the N-terminal of the normal enzymegave the following sequence:trp-arg-asp-leu-ser-gly-hisWhen the cDNA was sequenced by the Sanger method utilizing ddCTP, the following productswere obtained:TetranucleotideHexanucleotideNonanucleotideDecanucleotideDodenucleotideOctadecanucleotideNonadecanucleotide21-nucleotideWhat is the sequence of the bases in the mRNA coding for the peptide above?

Sanger DNA sequencing is carried out using ddCCTP for the chain termination. The given peptide is…

Answered: Failure of anti-oxidant function…

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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Eukaryotic elongation factor 2 is inhibited by ADP ribosylation catalyzed by diphtheria toxin. What other G proteins are sensitive to this mode of inhibition?
1 2 Glycogenin is a homodimer of 37 kDa subunits. (Homodimer means identical subunits of type a that form a dimer of type a2). Glycogenin has a chain of a(1,4)-linked units of glucose attached to the sidechain of a tyrosine residue. The chain of a(1,4)-linked glucose units is a primer for the initiation of glycogen synthesis by glycogen synthase. Assume the dimer is stable and not in equilibrium with monomer subunits. Which of the answers below are plausible pathways for attaching or building the primer chain of glucose units? The branching enzyme attaches a chain of 7 glucose units to the tyrosine sidechain of glycogenin. 0 0 0 0 000 The transferase attaches 3 units of a(1,4)-linked glucose to the tyrosine sidechain of glycogenin. Glycogen synthase then extends the chain using UDP-Glc. 0 One glycogenin dimer builds the a(1,4)-llinked glucose chain on a subunit of another glycogenin dimer. -D-O Each subunit builds the a(1,4)-Ilinked glucose chain on the other subunit of the same dimer.…
Human ribonucleotide reductase has two allosteric sites, the S site and the A site. What is the function of each? How does this compare with the E. Coli enzyme discussed in the text?
Why is de novo biosynthesis of purines markedly elevated in patients with a deficiency in hypoxanthine-guanine phosphoribosyl transferase (HGPRT)? 5-Fluoruracil is converted to methotrexate by a DPD deficiency, leading to increased purine biosynthesis. HGPRT deficiency prevents purine salvage, leading to increased purine biosynthesis to make up for it. HGPRT increases pyrimidine salvage and thereby increases purine biosynthesis as a result. Increased purine biosynthesis is the result of ATP hydrolysis during the production of cyclic AMP.
Galactosidase enzyme is considered a better selectable marker. Justify the statement.
Can you check if A is correct and please help answer the following questions?
Indicate the presence of the the B galactosidase and permease. Please explain and follow the instructions in the picture
Can you answer all the parts to this question please A. Where does a low barrier hydrogen bond (LBH) form transiently during the serine protease mechanism? B. What part does this LBH play in the serine protease mechanism?
A child with coarse facies, corneal clouding, joint stiffness and mental retardation is found to have a Damage to this enzyme directly affects which of partial defect in N-acetylglucosaminotransferase. the following biochemical functions? A. Formation of polysomes B. Microtubule attachment to centrioles C. Synthesis of ribosomal RNA D. Targeting of enzymes for lysosomes E. Transport of sugars into mitochondria
Suggest a reason why the amino acids thyroxine and hydroxyproline are produced by posttranslational modification of the amino acids tyrosine and proline, respectively.
Treating a solution of ribonuclease with 2-mercaptoethanol and urea denatures the enzyme. If the 2-mercaptoethanol is removed, followed by the removal of urea, the ability of the enzyme solution to hydrolyse RNA is reduced by about 99%. What is the most plausible explanation for this observation? a. All of the RNase molecules have about 1% of their usual activity, due to changes to the organisation of disulphide bonds b. Random formation of disulphide bonds mean about 1% of the RNase molecules are 100% active whereas 99% have no activity c. Deprotonation of histidine in the active site of the enzyme means that only about 1% of the enzyme molecules are active d. Deprotonation of histidine in the active site of the enzyme means that all of the enzyme molecules have 1% of their usual activity
Cystic fibrosis is genetic disease caused by mutations in the CFTR gene. The consequence of this is production of an abnormal transmembrane protein that is responsible for producing sweat, mucus, and digestive fluids. Please mention the process involved in protein production, whether or not those process(s) have occurred, and their end products.

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