6-Diazo-5-oxonorleucine (DON) irreversibly inhibits glutamine-dependentamidotransferases.CH=N+=N-C=0CH,CH,|H-C-NHCOO(a) Which intermediate or intermediates in purine nucleotide biosynthesiswould you expect to accumulate in DON-treated cells?(b) Which participants in pyrimidine synthesis?(c) Speculate on the mechanism by which DON inhibits these enzymes.

Introduction: DON is a water-soluble glutamine enemy which was separated initially from Streptomyces…

Answered: 6-Diazo-5-oxonorleucine (DON)…

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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6-Diazo-5-oxonorleucine (DON) irreversibly inhibits glutamine-dependent amidotransferases. (a) Which intermediate or intermediates in purine nucleotide biosynthesiswould you expect to accumulate in DON-treated cells?(b) Which participants in pyrimidine synthesis would you expect toaccumulate?(c) Speculate on the mechanism by which DON inhibits these enzymes.
TPCK and TLCK are irreversible inhibitors of serine proteases. One ofthese inhibits trypsin and the other chymotrypsin. Which is which? Explainyour reasoning. Suggest the effects of each of the following mutations on the physiologicalrole of chymotrypsinogen:(a) R15S(b) C1S(c) T147S
The following amino acids that are often found inside globulin molecules are () A, Tyr B, Phe C, Asn D, Glu True of false 1. In the de novo synthesis of purine nucleotides and pyrimidine nucleotides, base rings are first synthesized and then corresponding nucleotides are formed with phosphoribose. () 2. Transcription is the process of transferring genetic information from DNA to RNA. DNA is synthesized under the catalysis of RNA polymerase, and the direction of synthesis is from the 5 'end to the 3' end. () 3. The change of protein conformation is caused by the breaking of covalent bonds within the molecule. () 4. In very high and very low pH solutions, amino acids exist mainly in non-ionic form. () 5. The active center of an enzyme usually consists of several amino acid residues adjacent to each other in the primary structure. ()
3) Histone deacetylases (HDACs) are zinc-dependent enzymes that catalyse the conversion of acetyllysine to lysine. e) HN a) Propose the mechanism for the HDAC-catalysed reaction. b) What is the role of zinc ion in HDAC catalysis? c) d) f) HDAC NH₂ Draw the pH-activity profile for HDAC-catalysed conversion of acetyllysine to lysine. Explain. Suggest two acetyllysine analogues that are substrates for HDACs. One should be a better substrate than acetyllysine, whereas the other one should be a worse substrate than acetyllysine. Explain. Mutations in the HDAC sequence could lead to a loss of the catalytic function. Which mutations are problematic? Lysine acetylation is a reversible reaction using acetyl-CoA as a co-substrate. Which coenzymes are required for synthesis of acetyl-CoA in nature? Propose the mechanism.
When hyaluronan synthase from Pasteurella multocida was expressed in E. coli, the bacteria spun out a capsule of hyaluronan. This reaction was analyzed using purified membrane fragments containing the hyaluronan synthase, a radio-labeled tetrasaccharide acceptor (Part A), along with the activated forms of the sugar subunits: UDP-N-acetylglucosamine and UDP-glucuronic acid. In short incubations with the complete mixture, the tetrasaccharide primer elongated by several units, although only odd-numbered chains were visible (Part B lane 2). If one or both activated sugars were left out, the results shown in lanes 3-5 (Part B) were obtained. Why do you suppose that only odd-number chains are visible in your assay? (A) ACCEPTOR nonreducing end HO- HO OH COO glucuronic acid (GICUA) HO- CH3 T C=O I NH CH₂ OH N-acetylglucosamine (GlcNAc) COO но- HO OH OH I CH₂ reducing end NH C=O CH3 Choose one: O A. Synthase adds GlcNAc much more slowly than it adds GICUA. O B. One of the monosaccharide…
Most bacterial mutants that require isoleucine for growth also require valine.Why? Which enzyme or reaction would be defective in a mutant requiringonly isoleucine (not valine) for growth?
Why Phenylmethylsulfonyl fluoride (PMSF, shown in Fig.) does not inhibit aspartate protease as potent as serine protease?
You have an unknown heptapeptide that gives the following amino acids after acid hydrolysis (2M.2K,R, A,P) treatment with CNBr gives hormoserine lactone (M*), a tetrapeptide (2K,M*,A) and (P,R). Treatment with trypsin gives free P, free K, (A,K,M) and (R,M). what is the sequence of amino acids for the heptapeptide? show work.
An enzyme that catalyzes disulfide– sulfhydryl exchange reactions, called protein disulfide isomerase (PDI), has been isolated. PDI rapidly converts inactive scrambled ribonuclease into enzymatically active ribonuclease. In contrast, insulin is rapidly inactivated by PDI. What does this important observation imply about the relation between the amino acid sequence of insulin and its threedimensional structure?
The melanocyte-stimulating peptide hormone a-melanotropin has the following sequence: Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val (a) Write the sequence using the one-letter abbreviations. (b) Calculate the molecular weight of a-melanotropin, a da'
Which of the following regulatory mechanisms will specifically inhibit pyrimidine synthesis (and not also purine synthesis)? (A) allosteric regulation of aspartate transcarbamoylase by CTP(B) allosteric regulation of aspartate transcarbamoylase by ATP(C) synergistic inhibition of PRPP synthetase by AMP/GMP/IMP(D) synergistic inhibition of PRPP amidotransferase by AMP/GMP/IMP (E) feedback inhibition of ribonucleotide reductase by dATP
What would be the effect on the activity of phosphofructokinase of the mutation of Asp103 to the unusual amino acid shown below? Explain in terms of actual structures of the side chains of Asp and this unusual amino acid.

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