LECTURE SEATWORKCLASSIFY THE FOLLOWING ENZYMES6. Ptyalin7. Lactase8. Creatine phosphokinase1. Sucrase2. Trypsin3. Catalase4. Aspartate anminotransferase 9. 5-alpha reductase5. Cellulase10. Amino peptidase

There are 6 different classes of enzyme based on their action on the substrate.They are: 1.…

Answered: LECTURE SEATWORK CLASSIFY THE FOLLOWING…

World of Chemistry

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Author:Steven S. Zumdahl

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Chapter21: Biochemistry

Section: Chapter Questions

Problem 26A

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Write a brief description of the relationships among each of the following groups of terms or phrases. Answers to the Concept-Linking Exercises are given at the end of the chapter. Enzyme, enzyme substrate, active site, induced fit model
The human body has an average pH of about 7 and a temperature of about 37C. Use graphs to illustrate enzyme activity in the human body as a function of the following: a. Substrate concentration b. Enzyme concentration c. pH include pH optimum value d. Temperature include temperature optimum value
The process by which an enzyme acts on the substrate can be described by the: a. lock-and-key model. b. enzyme-and-substrate model. c. enzyme folding model. d. catalytic model.
In the multienzyme sequence shown below, molecules of D are able to fit to the enzyme E1 and prevent the conversion of A to B. What is this action of E called? AE1BE2CE3D a. effector inhibition b. allosteric inhibition c. feedback inhibition d. competitive inhibition by nonproduct
Would alpha-D-glucopyranose and alpha-D-fructopyranose be equally likely to be the substrate for a given enzyme? Refer to both shape and noncovalent interactions in your answer. Make one generalization about protein-carbohydrate interactions
Lecture seatwork classify the following enzymes 1.sucrase 2.trypsin 3.catalse 4.aspartate aminotransferase 5?cellulase
How does the near attack conformation (NAC) contribute to enzyme function?
Which statement(s) is(are) true about carbonic anhydrase enzyme?A. Carbonic anhydrase enzyme controls the production of carbonic acid.B. Carbonic anhydrase enzyme controls the pH of human blood.C. Zn metal is present in the catalytic site.
How can the Michaelis constant (Km) be identified and used to represent the affinity between the enzyme and the substrate?
Which interaction(s) is/are involved in the primary structure of a protein (choose all that apply)? a. hydrogen bonding b. salt bridge c. hydrophobic effects d. covalent peptide bond
It is known that the amino acid at position 523 of the cyclooxygenase enzyme is part of the active site. In the isoenzyme COX-1, this amino acid is isoleucine, whereas in COX-2, it is valine. Suggest how such information could be used in the design of drugs that selectively inhibit COX-2.
Which protein folding interaction(s) is/are most likely to occur on the outside of a protein pocket in water (choose all that apply). a. hydrogen bonding b. hydrophobic effects c. salt bridge

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LECTURE SEATWORK CLASSIFY THE FOLLOWING ENZYMES 6. Ptyalin 7. Lactase 8. Creatine phosphokinase 1. Sucrase 2. Trypsin 3. Catalase 4. Aspartate anminotransferase 9. 5-alpha reductase 5. Cellulase 10. Amino peptidase