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.
Q: What effect is seen on a Lineweaver-Burke graph when a competitive inhibitor is added to an…
A: Competitive inhibition is an enzyme inhibition process where an inhibitor molecule (similar to the…
Q: Place the following enzymes in the correct order of action RNA 5' triphosphatase RNA polymerase II…
A: The newly synthesised mRNA is called the primary transcript. Before the primary transcript can be…
Q: Test I. MULTIPLE CHOICE: Read the statement carefully. use CAPITAL letters. 1. It refers to the…
A: Note: Hi! Thank you for the question. We are authorized to answer one question at a time. Since you…
Q: Exergonic and endergonic biochemical reactions; the role of ATP and other macroergic substances in…
A: INTRODUCTION : ATP - Adenosine triphosphate, it is the main energy currency or units, which is…
Q: Consider the enzyme, ATCase. All are true except: It's K effectors are ATP and CTP It is a K…
A: ATCase (Aspartate carbamoyltransferase) is an enzyme which catalyzes the first step of the synthesis…
Q: A patient weighing 38.4 pounds presents with a bacterial infection and is prescribed a course of…
A: A multitude of bacterial infections can be treated with the antibiotic amoxicillin. These include…
Q: Which of the following is CORRECT? A) Pyruvate kinase requires Mg2+ for maximal activity. B) A small…
A: Pyruvate Kinase is an enzyme which catalyzes the last step of glycolysis, i.e, conversion of…
Q: 2. What is the total yield from one molecule of glucose to two molecules of L-malate? A. 2 ATP/GTP,…
A: Glucose is converted to L-malate via the following pathway: 1. Glycolysis: 1 glucose is converted to…
Q: Which of the following statements is FALSE regarding oxidative phosphorylation? The pH is higher in…
A: Cellular respiration is a collection of three metabolic pathways that generate ATP by oxidation of…
Q: ATP stock (50 µM): Make pre-dilutions with 20, 15, 10, 5, 2,5 and 1,25 µM ATP (1000 μL of each)…
A: Molarity is a way of representing the concentration of a solution. Molarity is the number of moles…
Q: QUESTION: For each enzyme identify the transition-state inhibitor analog by drawing a circle around…
A: Whenever a reaction takes place there are reactants and they form products but in between, during…
Q: Given that the reduction potential Eo'= -320, +10, +816, and +50mV for NAD+, fumarate, O₂ and…
A: An oxidizing species is the substance that donates electrons, and a reducing species is the…
Q: Which of the following laws of matter best describes the statements on sulfide minerals? Select one:…
A: INTRODUCTION : Sulfide minerals - They are a class of minerals consisting of sulfide or disulfide…
Q: What effect does a negative effector have on the graph of reac- tion rate (V) vs. [substrate] for an…
A: INTRODUCTION : Allosteric enzymes : Allosteric enzymes are those enzymes which have an additional…
Q: Consider the structure of the tripeptide below. H H₂N-C-C- 0=6 CH₂ CH₂ C=0 1 NH₂ pH 5: O pH 10: H O…
A: The given peptide has three amino acids joined by the peptide bond. There are three ionizable groups…
Q: Kwon Soon-young was asked by his CHEM 160.1 lab instructor to determine the isoelectric pH of an…
A: Proteins are composed of twenty standard amino acids attached together via peptide bonds. These…
Q: vo (μM/min) 25 20 15 10 5 0 7 VO (μM/min) VS pH 8 pH 9.5 10.4
A: Enzymes are the catalysts that function to increase the rate of reaction by decreasing their…
Q: 1. What is the sequence of the heptapeptide produced upon treatment with trypsin? Fill each blank…
A: Specific enzymes have specific cleavage point in amino acids. Chymotrypsin is serine…
Q: Which of these are components of animal fatty acid synthase (FAS)? B-ketoacyl reductase enoyl…
A: The majority of healthy human tissues primarily create new structural lipids from circulating…
Q: A peptide has the following amino acid composition: 2 Met, 2 Phe, 2 Glu, 1 Arg, 1 Lys, 1 Val, 1 Leu,…
A: Recall that: Amino acid sequences are written with N-terminal amino acid on the left and C-terminal…
Q: 5. In the early days of protein biochemistry, these proteins were described using "operational…
A: Operational definition is applicable to many things in our everyday life. It is most popularly used…
Q: The proton-motive force is a measure of the potential energy generated across the mitochondrial…
A: INTRODUCTION : Proton-motive force : It is a measure of the potential energy generated across the…
Q: AMP is an activator of fructose 1,6-bisphosphatase (FBPase-1) True False
A: Glycolysis is the process by which one molecule of 6 carbon glucose is broken down into 2 molecules…
Q: 1. Under what circumstances in the cell would the entire pentose phosphate pathway be carried out…
A: In animal tissues, glucose has two possible fates: be oxidised into carbon dioxide and water by…
Q: More energy comes out of glucose degradation if pyruvate proceeds to the mitochondria for oxidative…
A: Degradation of glucose is termed as glycolysis which is a catabolic pathway in which 6 carbon…
Q: Describe the biological functions of lipids. What factorscan affect the transition temperature (Tm)…
A: Lipid is a biomolecule which is soluble only in nonpolar solvents. They are hydrocarbons which…
Q: State what each of the following symbols stands for, be specific. 4. M 5. SD 6. α
A: Introduction There are various symbols are used in science. Scientific writing requires various…
Q: 018 You have isolated a gene that spans a total of 1800 nucleotides. The gene contains 400…
A: Genes are the sequences of nucleotides attached together through phosphodiester bonds. Genes are…
Q: 384 Hemoglobin: Allostery and Evolution Q5.1 - 2,3-BPG is a negative allosteric regulator of…
A: Hemoglobin (Hb) is a protein that is found in red blood cells. A specific protein called haemoglobin…
Q: What is expected theoretical number of copies of DNA molecules after 28 cycles in a PCR experiment?…
A: INTRODUCTION: DNA : Its fullform is Deoxyribo nucleic acid and It has a double stranded helix…
Q: Question 9 Which of the following fatty acid does have greater solubility in wat O 16:0 O 18:0 O…
A: Fatty acids are a class of lipids that are nonpolar and are insoluble in water. The naturally…
Q: Chemistry Most of the reactions in gluconeogenesis are the simple reversal of the ‘forward’…
A: In gluconeogenesis pathway, the formation of phosphoenolpyruvate from oxaloacetate is catalyzed by…
Q: 1. Glucagon is a hormone that involves in the regulation of carbohydrate homeostasis.…
A: Proteins are made up of amino acid residues linked via a peptide bond. A peptide bond between two…
Q: What is the charge on the following peptide at standard biochemical pH? S-Y-D-F-K-I-V-F-L-L +2 -1 O…
A: Peptides are composed of amino acids. Amino acids are biomolecules with an alpha carbon bonded to an…
Q: 2. You made a pH=2.5 buffer solution by mixing NaOH and glycine to give a solution that is 0.20 M in…
A: Dissociation of a weak acid is mathematically described by the Henderson-Hasselbalch equation: pH =…
Q: 4. RNAse A cleaves the phosphodiester backbone of RNA. Draw its mechanism.
A: INTRODUCTION : RNA - It is called Ribonucleic acid, It is a nucleic acid which is present in all…
Q: Lactate dehydrogenase isoforms contain "H" and "M" subunits. In total, how many subunits are found…
A: - A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. - Enzyme…
Q: a) Draw the A-T and G-C base pairs. - Label the bases…
A: DNA are polymers of nucleotides. A nucleotide consists of a nitrogenous base(A, T, G, C) attached to…
Q: 1. Why do proteins become polycations at extremely low pH and become polyanions at very high pH? 2.…
A: Proteins are biological macromolecules formed by monomers of amino acids. The amino acids have side…
Q: What are the key differences between DNA synthesis (in the context of DNA replication) and RNA…
A: DNA is the genetic material. Replication is the process that copies the DNA to produce identical…
Q: Metabolic pathway characteristics: a. Give one example of an amphibolic pathway. b. What…
A: Metabolic pathways are a series of process which includes chemical reactions occurring in a cell.…
Q: 8. Anaplerotic and amphibolic reactions in TCA.
A: In aerobic condition, pyruvate in the presence of pyruvate dehydrogenase complex produces Acetyl…
Q: DNA: Explain nick translation and strand displacement
A:
Q: Biochemistry:Lable out the main difference of Primary,secondary,tertiary,and quatrenary structure.
A: Proteins are biomolecules composed of amino acids. Proteins have four levels of conformations known…
Q: Calculate the pI of the peptide KLMRDSP (pKa = 3.5, 3.9, 9.5, 10.0, 12.5).
A: The amino acids contain ionizable groups. The ionic form of these groups depends upon the pH of the…
Q: What is ATP? in 5 sentences Why is ATP important in the body? in 5-7 sentences
A: There are many forms of energy. But living system needs one form of energy i.e., chemical energy.…
Q: How many cycles of the synthesis pathway are needed to produce lauric acid, C₁1H23COOH? ||…
A: The production of triglycerides from acetyl-coenzyme A (acetyl-CoA) subunits is known as…
Q: Which one of the following amino acids is phosphorylated during the process of promoter clearance by…
A: The transcription of genes leading to the synthesis of proteins inside the cells is carried out by…
Q: i) Re-arrange with the Michaelis Menten equation so it involves the ratio [S] Show all steps…
A: Michaelis-Menten equation A mathematical model called the Michaelis-Menten equation is used to…
Q: 31. Margarine is made from vegetable oil by a chemical process. Do you suppose this process converts…
A: Margarine is a product derived from vegetable oil, obtained by the hydrogenation,…
Trending now
This is a popular solution!
Step by step
Solved in 2 steps
- 7. 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 Rengent5. Shown below are the first steps in the mechanism of a cysteine protease, which catalyses amide bond hydrolysis in a similar manner as serine proteases. (a) Complete this mechanisms, and (b) sketch the approximate reaction coordinate diagram for this catalyzed reaction relative to the uncatalyzed proteolysis. HN N HN cysteine proteasecomplete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.
- 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?(i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?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).
- 1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial wall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:1.Ala-Phe-Lys-Val-Val-Glu From the above polypeptide, what amino acid/s go/goes inside the cell after the following treatment: Chemotrypsin, thermolysin, then finally pepsin. What protein is left undigested? Write the primary structure of the undigested protein? 2.K-V-F-W-P-L-A-Y a.Chemotrypsin treatment b.Trypsin treatment c.Pepsin treatment d.Thermolysin treatment 3.Total acid hydrolysis of a pentapeptide complemented by total alkalinehydrolysis yields an equimolar mixture of 5 amino acids listed alphabetically, ala-cys,lys,phe,ser. N-terminal analysis with phenylisothiocyanate (PITC) generate PTH-ser. Trypsin digestion produces a tripeptide where N-terminal residue is cys and a dipeptide with ser as its N- terminal.Chemotrypsin digestion of the above tripeptide yields ala plus another dipeptide. A.What is the amino acid sequence of the tripeptide B.What is the amino acid sequence of the dipeptide derived from trypsin digestion? C.What is the primary structure of the original…1.The diagram below shows an outline of the aminotransferase mechanism that skips the specific steps that show how electrons flow when a Schiff base is formed or is hydrolyzed. Using the mechanistic details given below A. Draw the mechanism for Enzyme- PLP Schiff base formation using pyridoxal and the lysine amine group using arrow to indicate electron flow. B. Draw the mechanism for hydrolysis of the Schiff base to form the a-keto acid, which is the reverse of the first reaction. Stage 1 Lys residue 2-O,PO- Enz Amino acid Lys residue (CH2)4 (CH₂2)4 H R-C-COO R- NH₂ NH₂ R-C-COO *NH₂ H H- 2-0,PO- 2-0,PO- A. show how this forms Stage 1 Lys residue Enz (CH2)4 HO 2-O,PO Enzyme-PLP Schiff base OH Amino acid-PLP Schiff base (aldimine) LOH 2-0₂PO- OH 20,PO- a-Keto acid COO Ketimine a-Keto acid 2-0,PO- R-C- NH₂ B. show how the a-keto acid forms a-Keto acid H Enzyme-PLP Schiff base الرواية وطري Ketimine Pyridoxine (vitamin B6) Pyridoxal phosphate (PLP) Pyridoxamine phosphate Stage 2 Amino acid…
- 11. This below notation represents a Bi-Bi reaction. Aspartate Oxaloacetate a-Ketoglutarate Glutamate Enzyme Enzyme E (E-NH3) (oxaloacetate) (E-NH3) (E-NH3) (a-ketoglutarate) E (aspartate) (glutamate) In this rection, in which step the ternary complex is formed? Briefly explain your answer.2. ( the active site in the Michaelis complex of a-chy- motrypsin and a polypeptide substrate. Describe briefly the catalytic or structural roles of the : To the right is a schematic diagram of His $7 residues listed below: HOSer 195 (а) Ser195 AAn-C-ÇH-NH-Ç ÇH-NH -AAn R H H. -N- 195 193 Gly Ser (b) His57 (c) NH groups of Gly193 and Ser195 (d) The most favorable side chain R for binding (e) Identify the scissile bond with an arrow, i.e., the bond in the peptide substrate that is cleaved as a result of the catalytic action of the enzyme. You can point to it on the diagram above.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.