thymine nucleotides
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- 3. Solve the sequence of an oligopeptide 7 residues long which gave: Asp Leu Lys Met Phe Tyr The following facts were observed: a. Trypsin treatment had no apparent effect b. The PTH derivative from Edman degradation was c. Brief chymotrypsin treatment yielded several products including but not limited to a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys, and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and a free Lys. Instructions Make use of the table below to determine the sequence of the mystery protein.Protease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. O Macmillan Learning On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a metalloprotease. Metalloproteases H R₁ HN Zn Enz 2+ R₂ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing. Select Draw Templates Groups More B - H Enz H H с R1 | : HN O | Zn 2+ B R2 N Zn Erase7. Chalcone isomerase catalyzes the reaction illustrated below. A series of modification experiments were performed on this enzyme to identify which amino acid residues might be in the active site and which might promote the cyclization reaction. OH Ho. Но Explain the following results: A) Acetic anhydride treatment inhibited enzyme activity. B) Pyrocarbonate inhibited activity and was found to modify 7 residues. However, this enzyme only contains 6 His and modification of these did not affect activity. C) lodoacetate inhibited activity but this effect coult be decreased in the presence of substrate or product. D) Methane methanethiol sulfonate modified the enzyme but did not inhibit catalytic turnover. In addition, this modification was reversed in the presence of B-mercaptoethanol. keNyons Rengent
- 1 ).Which of the following accurately describes substrate specificity for serine proteases? A.The binding cleft B.Mg2+ metal activated enzyme C.The catalytic triad D.Facilitates redox chemistry E.Stabilizes the transition state 2). Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? select all that apply leucine aspartic acid histidine lysine Please answer both correct i will give u upvote.Describe how the concentrations of the four deoxyribonucleotides are balanced by ribonucleotide reductase.2. Amino acid analysis of the a heptapeptide gave the following residues: Asp Glu Leu Lys Met Tyr Trp NH4+. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was OH H C-C-CH₂ H. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Glu, Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a tetrapeptide that had a net positive charge at pH 7 and tripeptide that had a zero net charge at pH 7. What is the amino acid sequence for this heptapeptide?
- 10. Chymotrypsin is a serine protease enzyme. The Km for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8*102, and the Km for the reaction of chymotrypsin with N- acetyltyrosine ethyl ester is 6.6*10“ M. catalytic triad Ser 195 His 57 Gly 193 N-H OH R-N- Ca N-H O-C- Asp 102 N-acetyl valine N-acetyl tyrosine Chymotrypsin Active Site a. What is the nucleophile here and how is it activated? b. Which substrate has an apparent higher affinity for the enzyme. c. Propose a reason for the difference in affinity based on the shape of each of the substrates (see active site figure, cleaves on the C-side of aromatic residues).5. Consider the reaction for assembly of a tetrapeptide from for amino acids: Serine + Proline + Alanine + Methionine ----> SPAM tetrapeptide Is this reaction anabolic or catabolic? Is this a positive or negative delta G reaction? List at least three other terms you could use to describe this reaction. 6. Consider the reaction: Glutamic acid + Ammonia + ATP ----> Glutamate + ADP + Pi Is this reaction anabolic or catabolic? Is this a positive or negative delta G reaction? This is actually an example of a coupled reaction! Briefly, explain why reaction coupling is required, and how it works in this example.The enzyme cytidine deaminase catalyzes the conversion of cytidine to uridine. Cytidine deaminase catalyzes the reaction through an addition of water across the cytidine 3,4-bond, forming a tetrahedral intermediate followed by the elimination of NH3 to form the product uridine. This is like the addition-elimination mechanism that we studied for adenosine deaminase. Cytidine deaminase НО. NH₂ N пOH OH cytosine R + H₂O cytidine The Km value for the substrate cytidine is 2.5 × 10-4 M, and the K; for competitive inhibition by the product uridine is 2.5 × 10-³ M. N R A reduced derivative of the product, 3,4,5,6-tetrahydrouridine was shown to be a fully reversible competitive inhibitor with a Ki of 2.4 x 10-7 M, a value approximately 10,000 times lower than that of the product uridine. NH₂ NH uridine HO. N R R = D-ribose HOH OH uridine 3NH uracil ring numbering H NH H H + NH3 H OH H 3,4,5,6-tetra- hydrouridine a.) Draw a structure of the intermediate that we predict to form during the…
- NH₂ CH3 Methyltransferases NH₂ OH OH S-Adenosylmethionine (SAM) Transamination Phosphate transfer Protein Acetyl transfer Transmethylation CH3 DNÁ CH3 NH₂ What metabolic reaction is best represented by this chemical equation? SAH-Hydrolase (SAHase) NH₂ OH OH S-Adenosyl-L-Homocysteine (SAH) I но. #M OH OH Adenosine NH₂ NH₂ SH Homocysteine1. Give TWO (2) examples of sterols responsible for the synthesis of Vitamin D. How these sterols can be converted into Vitamin D? 2. Geranylgeranyl pyrophosphate (GGPP) is a universal precursor for all diterpene/diterpenoids. How GGPP is converted to linear, monocyclic, bicyclic and tricyclic diterpene/diterpenoids? Explain.1. Consider the three-dimensional model of the tertiary structure of an enzyme below. Amino acids involved in binding are shaded blue, and amino acids involved in catalysis are shaded red. A. Suppose research has shown that amino acid 82 in the red shaded region is lysine, an amino acid with a positively-charged side chain. This lysine is critical for catalysis. Other studies have found that amino acids 12 and 62 in the blue region are both phenylalanine, an amino acid with a nonpolar side chain, and are critical for substrate binding. These amino acids are relatively close in the active site but are separated by 20-70 amino acids in the primary structure. Using what you know about protein structure, explain how amino acids separated in the primary structure can come close together in the active site. B. Use this information and figure 4.2 in your book to answer the following questions: Do you think changing amino acid 82, lysine, an amino acid with a positively-charged side…
