Answer:1.2.3.4.5.6.7.8.9. I. OBJECTIVESSolve problems involving reaction mechanism in chemical kineticsCite and differentiate types of catalystsII. GENERAL INSTRUCTIONSAnswer the following items.1. Give an example of a catalyst and its importance. Examples in the material (slideshow andvideo) will not be accepted.2. Identify the enzymes in the Tricarboxylic Acid Cycle below.Acetyl-CoA COASH-co0HO-C-CDOHE-cooOxalcacetateNAHCitrate000-000-co0-coo-cooL-Malatecoocis-AconitateTricarboxylicAcid CyclecooFumarateIsocitrateNADHSuccinateCOASHa-KetoglutarateSCalSuccinyl-CoA

Tri carboxylic acid cycle or the citric acid cycle, TCA cycle or the Krebs cycle is a series of…

Answered: II. GENERAL INSTRUCTIONS Answer 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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We saw the oxidation/reduction of malate to/fro oxaloacetate in two pathways that we looked at: _____________________________________ and _________________________.
Summaries of two clinical case studies follow. For each case determine which enzyme isdefective and designate the appropriate treatment, from the lists provided at the end of theproblem. Justify your choices. Answer the questions contained in each case study. 15 marksCase A The patient complains of painful muscle cramps when performing strenuous physicalexercise but has no other symptoms. A muscle biopsy indicates a muscle glycogen concentrationmuch higher than normal. Why does glycogen accumulate?Case B The patient is lethargic, her liver is enlarged, and a biopsy of the liver shows largeamounts of excess glycogen. She also has a lower than normal blood glucose level. What is thereason for the low blood glucose in this patient?
Case Study: Case Study: Catalase Activity Catalase H,O, 0 + O2 (2) Catalase is an enzyme that converts hydrogen peroxide (H,O) to oxygen and water. An experiment investigated the effect of temperature on the rate of the catalase reaction Small (10 cm) test tubes were used for the reactions, each containing 0.5 cm of enzyme and 4 cm of hydrogen peroxide. Reaction rates were assessed at four temperatures (10°C, 20°C, 30'C. and 60 C). For each temperature, there were two reaction tubes (e.g. tubes 1 and 2 were both kept at 10°C). The height of oxygen bubbles present after one minute of 10°C 20°C 30°C 60°C Height of охудen bubbles 4 cm H,02+ 0.5 cm erzyme reaction was used as a measure of the reaction rate: a laster reaction rate produced more bubbles. The entire experiment, involving eight tubes, was repeated on two separate days. Tubes Tubes Tubes 1 & 2 Tubes 3 & 4 5 & 6 7 & 8 1. What is the purpose of this experiment? inrestrgatee effect of demperalure on the rate ot he 2. Write a…
Answer the ff. questions: 1. To which class does each enzyme belong? Explain your answers. a.) pyruvate decarboxylase b.) alanine aminotransferase c.) alcohol dehydrogenase d.) hexokinase 2. Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis? 3. Some plants contain compounds that inhibit serine proteases. It has been hypothesized that these compounds protect the plant from proteolytic enzymes of insects and microorganisms that would damage the plant. Tofu, or bean curd, possesses these compounds. Manufacturers of tofu treat it to eliminate serine protease inhibitors. Why is this treatment necessary?
Name: Sincere Frias Date: (0/2/2od0 Period Ced th nzy ck. Enzyme Models & Factors Affecting Enzyme Action PART I – Lock and Key Model st In this part you will construct models of enzymes. Remove the last page and cut all shapes out. 2. The different shapes will represent both enzymes and substrates. 3. Match up as many of the pieces as you can. 1. Questions 1. The enzyme maltase combines the substrates h ydrolysis + Starch molecule to produce the disaccharide maltose. 2. The enzyme ATPase combines the substrates_molecule and to produce the ATP (Adenosine TriPhospate). Iriglyceride 3. The enzyme lipase works on the substrate called 4. The enzyme phosphatase works on the substrate called 5. What is the relationship between the substrate and the enzyme?
m BIO101 Short EXAM First session X G Google om/moodle/mod/quiz/attempt.php?attempt%3D1313727&cmid%3D298536 e on the bookmarks bar. Import bookmarks now... AL BIOLOGY I/ ill courses GENERAL BIOLOGY I BIO101 Short EXAM First sess Time left 0:21:42 If an enzyme in solution is saturated with its substrate, the most effective way to obtain a higher reaction rate is to: O a. add more substrate O b. heat the solution to 95°C O c. add more of the enzyme O d. All of the options are correct O e. add a noncompetitive inhibitor Next page vity Jump to.. ents 51°F Light rair
I. Predict the outcome of the following reactions. If positive write what will you observe (color, name of the product). If negative, explain the reason why. NH Orcinol но- NH2 A 1.) OH 'NH но NH A 2.) ОН ОН HO-P-O-P-O он (NH4)4MOO4 OH OH OH Conc. HNO; 3.) OH
PRODUCTS. Match the name of the product with the biochemical reaction. Products may be used more than once. Tests may require more than one answer. a. 2,3-butanediol b. ammonia c. fatty acids d. indole e. molecular oxygen f. phenylpyruvic acid catalase phenylalanine deamination triglyceride hydrolysis tryptophan degradation urea hydrolysis Voges-Proskauer test
5. Matching Type Match Column A with Column B. Write your answer on the space provided. CAPITAL letters only. Column A Column B 1.. Citrate → Isocitrate 2. Fumarate → Malate 3. Fructose-1,6-bisphosphate → G3P and DHAP 4. PEP → Pyruvate 5. a-Ketoglutarate → Succinyl-CoA 6. Substrate-level phosphorylation 7. Oxidative decarboxylation 8. Reduction 9. Isomerization 10. Condensation 11. Fumarate → Malate 12. Citrate → Isocitrate 13. Succinate → Fumarate 14. Succinyl-CoA → Succinate 15. Malate → Oxaloacetate 16. Pyruvate → Acetaldehyde 17. Pyruvate → Acetyl-CoA 18. PEP → Pyruvate 19. 2-Phospoglycerate → PEP 20. Glucose Glucose-6-phosphate A. Succinate dehydogenase B. Succinyl-CoA synthetase C. Malate dehydrogenase D. Fumarase E. Citrate synthase E. Isocitrate → a-Ketoglutarate F. 3-Phosphoglycerate → 2-Phosphoglycerate F. Aconitase G. Acetyl-CoA + Oxaloacetate → Citrate G. Glycolysis H. Pyruvate → Lactate I. Glucose-6-phosphate → Fructose-6-Phosphate K. Kreb's cycle U. Enolase V. Hexokinase…
What are the corresponding answers, respond briefly, site sources Enzyme; Triacylglycerol Lipase Enzyme Official Name (write N/A if not applicable) Enzyme Official Number (4 digits) Simple or Conjugated Enzyme (specify cofactor if applicable) Type of Reaction Catalyzed Substrate Optimum pH Optimum Temperature Function/s Disease (give 1 and describe briefly) Enzyme: Urease Enzyme Official Name (write N/A if not applicable) Enzyme Official Number (4 digits) Simple or Conjugated Enzyme (specify cofactor if applicable) Type of Reaction Catalyzed Substrate Optimum pH Optimum Temperature Function/s Disease (give 1 and describe briefly)
instructions: add the drawings to these given answers please. its urgent answers are given as follows A. The tetrahedral intermediate attacks the carbonyl carbon of the peptide bond, cleaving it and forming a new peptide bond with the nitrogen of aspartate. This process is repeated for each peptide bond in the substrate, resulting in the formation of the product and free enzyme. In this example, the product is a dipeptide and free enzyme. In addition to forming a tetrahedral intermediate, the catalytic mechanism of papain involves general acid-base catalysis through His57 in Asn152. The amino group in Asn152 deprotonates the hydroxyl side chain in Phe153, which is stabilized by hydrogen bonding. This deprotonation facilitates nucleophilic attack at the carbonyl carbon of the peptide bond in the substrate, resulting in a tetrahedral intermediate. His57 also protonates Asp102, stabilizing it as a general base to facilitate formation of the tetrahedral intermediate. The nucleophilic…
2 W 1 Z MacBook Air PRE-LAB ASSIGNMENT Enzyme - Functional Analysis Instructions: Read the Introduction section of the lab and watch the following video: https://www.youtube.com/watch?v=V6wHXtO9kIA. Then complete the questions below. 1. Define Enzymes. What type of macromolecules are enzymes? 2. What are two advantages of having enzyme-catalyzed chemical reactions in living cells? reaction? 3. What is a substrate? Where on an enzyme does the substrate specifically bind to during a chemical in each of following: 4. When an enzymatic reaction is in progress, do you expect to see an increase, decrease or no change (i) substrate (ii) product (iii) enzyme 5. How can you measure enzyme activity? 77

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II. GENERAL INSTRUCTIONS Answer the following items. 1. Give an example of a catalyst and its importance. Examples in the material (slideshow and video) will not be accepted. 2. Identify the enzymes in the Tricarboxylic Acid Cycle below.