BIOCHEM 423 Chapter Notes - Chapter 11.1: Anabolism, Organic Compound, Catabolism

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viridianhornet922

7 Dec 2018

School

UMASS-Amherst

Department

Biochemistry & Molecular Bio.

Course

BIOCHEM 423

Professor

Ma Fu

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Document Summary

[ complex substances are degraded to simpler molecules ] anabolism synthesis of complex organic molecules. Both can be subdivided into three stages , based on the complexity of metabolites involved . the intermediates and products of metabolism ] Stage i the interconversion of polymers and complex lipids with monomeric intermediates. Acids stage 2 : the interconversion of monomeric sugars , amino acids and lipids with still simpler organic compounds . Stage 3 = the ultimate degradation to , or synthesis tom , inorganic compounds , including cos. Hw and ntb a three important concepts a. Metabolism includes all reactions involved in generating and storing metabolic energy. C catabolic reactions and with using that energy in the biosynthesis . of how - molecular - weight compounds , or intermediates as well as energy - storage compounds l anabolic reactions ) Not included in intermediary metabolism is the biosynthesis of nucleic acids and proteins from monomeric precursors.

Related Questions

Need help with biology questions:

1. To increase the excretion of an acidic drug, what would you do to the urine?

	A.	Make it more basic
	B.	None of the above
	C.	Make it neutral
	D.	Make it more acidic

2. G-Protein coupled receptors directly act on which of the following secondary messenger molecules:

	A.	cAMP
	B.	ATP
	C.	ADP
	D.	GTP
	E.	None of the above or more than one of the above

3. Drug A and Drug B both produce the same level of biological/physiological response. Drug A produces this effect with 100 mg/kg dose. Drug B produces this effect with 50 mg/kg dose. Which of the following is true?:

	A.	Drug B is more efficacious than Drug A. Both drugs are equally potent.
	B.	Drug A is more efficacious than Drug B. Both drugs are equally potent.
	C.	Drug A and B are equally efficacious. Drug A is more potent than Drug B.
	D.	Drug A and B are equally efficacious. Drug B is more potent than Drug A.

4. The stomach has a ______ pH, whereas the small intestines have a _______ pH. The colon has an approximately ___________ pH.

	A.	High; low; neutral
	B.	Low; high; neutral
	C.	Low; neutral; neutral
	D.	None of the above

5. Which receptor is most likely to reduce norepinephrine levels when activated?

	A.	alpha 2 adrenergic
	B.	alpha 1 adrenergic
	C.	dopamine D1 receptors

6. Which of the following statements are FALSE?

	A.	If the Vd of a drug is between 60 and 80 L the drug has likely distributed to the total body water of a 200 kg man.
	B.	In the enterohepatic system the activity of bacteria to remove conjugates from a drug in the gut will decrease the clearance of the drug.
	C.	Lipid drugs are more likely to be reabsorbed by the kidney from the urine.
	D.	A weak basic drug (pKa = 6) will be mostly ionized in urine of a pH= 3 and only the non- ionized drug will be eliminated.
	E.	The major conjugate in Phase 2 metabolism is glucuronide.

7. Isoproterenol (Î²-agonist) is a vasodilator that increases HR. What happens to systolic and diastolic pressures upon IV administration of isoproterenol?

	A.	â systolic; â diastolic
	B.	â systolic; â diastolic
	C.	â systolic; â diastolic
	D.	â systolic; â diastolic
	E.	None of the above

8. If you want to increase the blood concentration of a drug A, you can perform which of the following procedures:

	A.	Inhibit Drug A metabolism with Drug B
	B.	Enhance Drug A reabsorption from renal proximal tubule by changing ionization of Drug A with Drug B
	C.	Allow competition of Drug B with Drug A for active renal secretion processes
	D.	Increase the binding of Drug A to serum albumin
	E.	All of the above

9. Which of the following describes Phase I metabolism?

	A.	Inactive products are always produced in this phase.
	B.	Large molecules such as glucuronic acid are conjugated to drugs in this phase.
	C.	This phase may produce active metabolites from prodrugs.
	D.	This phase only occurs in the liver.

10. Which of the following is NOT an enzyme involved in the biosynthesis of biogenic amines?

	A.	Phenylethanolamine N-methyl Transferase
	B.	Dopamine Î²-hydroxylase
	C.	Tyrosine dehydroxylase
	D.	DOPA decarboxylase
	E.	All of the above

11. Why would an antibiotic at the same concentration be more active against bacteria in water than in serum or plasma? (Activity is measured in a test tube)

	A.	activity of the antibiotic is increased in water.
	B.	due to drug-protein interaction in serum
	C.	the antibiotic is more stable in water
	D.	all of the above
	E.	none of the above

12. Ion channels are targets for drugs. Which drug class targets Na+ channels?

	A.	Benzodiazepines
	B.	Beta blockers
	C.	Local anesthetics
	D.	Antihypertensive drugs (cardiac and smooth muscle)
	E.	Glibenclimide (diabetic drug)

13. _________________ not metabolized by catechol-O-methyltransferase (COMT).

	A.	Dopamine
	B.	Epinephrine
	C.	Phenylephrine
	D.	Norepinephrine
	E.	All of the above are metabolized by COMT.

I JUST NEED SIMPLE/BASIC ANSWERS NOT LONG ANSWERS

1. Explain how life can be viewed at different levels of biological complexity.

2. Explain how researchers study biology at different levels, ranging from molecules to ecosystems.

3. Distinguish between discovery-based science and hypothesis testing, and describe the steps of the scientific method.

4. Tell whether a given topic or research study is about biology. Tell whether that study is discovery-based or hypothesis testing, or both.

5. If presented with a research study, propose what the Research Question was.

6. If presented with an example, tell whether a statement is a hypothesis, theory or law and why you think so.

Describe the general structure of atoms and their constituent particles.

Relate atomic structure to the periodic table of the elements. List the elements that make up most of the mass of all living organisms.

Explain how a single element may exist in more than one form, called isotopes, and how certain isotopes have importance in human medicine.

Compare and contrast the types of atomic interactions (bonds) that lead to the formation of molecules.

Tell which atoms and how many of each make up a given molecule (formula or diagram).

For a bond in a given molecule, tell whether the bond is covalent, and if it is, tell whether it is polar or nonpolar and why you think so.

Explain the concept of electronegativity and how it contributes to the formation of polar and nonpolar covalent bonds. Tell whether a given atom is electronegative or not, and why you think so. Label partial charges in a polar bond.

Draw five water molecules and label the atoms and bonds within and between the 5 molecules.

Describe how hydrogen bonding determines many properties of water.

List the properties of water that make it a valuable solvent, and distinguish between hydrophilic and hydrophobic substances.

Explain how water has the ability to ionize into hydroxide ions (OH^â) and into hydrogen ions (H⁺), and how the H⁺ concentration is expressed as a solution's pH.

Explain the properties of carbon that make it the chemical basis of all life.

Describe the variety and chemical characteristics of common functional groups of organic compounds.

Diagram how small molecules may be assembled into larger ones by dehydration reactions and how hydrolysis reactions can reverse this process.

List the four major classes of organic molecules and macromolecules found in living organisms

If shown a molecule, tell whether it is organic or not and how you know.

If shown an organic molecule, tell whether it is an amino acid, nucleotide, fatty acid, steroid, monosaccharide or disaccharide and how you know.

Distinguish among different forms of carbohydrate molecules, including monosaccharides, disaccharides, and polysaccharides.

Relate the functions of plant and animal polysaccharides to their structure.

List the several different classes of lipid molecules important in living organisms.

Diagram the structure of a triglyceride and explain how it is affected by the presence of saturated and unsaturated fatty acids. Explain why some fats are solid at room temperature, and others are liquid.

Discuss how fats function as energy-storage molecules.

Apply knowledge of the structure of phospholipids to the formation of cellular membranes.

Describe the chemical nature of steroids and give an example of their biological importance.

Give examples of the general types of functions that are carried out in cells by different types of proteins.

Explain how amino acids are joined to form a polypeptide, and distinguish between a polypeptide and protein.

Describe the levels of protein structure and the factors that determine them. If shown a protein diagram, label parts that represent its levels of structure. Tell what kind of research techniques are used to determine protein structure.

Outline the bonding forces important in determining protein shape and function.

Explain what domains are and their importance in proteins.

Describe the three components of nucleotides.

Distinguish between the structures of DNA and RNA.

Tell how certain bases pair with others in DNA and RNA.

Discuss the 4 major categories of organic macromolecules found in living things, including structure, function and location of each.

Compare and contrast the general structural features of prokaryotic and eukaryotic cells.

Outline the differences in complexity among bacteria, animal, and plant cells.

Describe how a eukaryotic cell can be viewed as four interacting systems: the nucleus, cytosol, endomembrane system, and semiautonomous organelles.

Explain how the proteome underlies the structure and function of cells.

Analyze how cell size and shape affect the surface area/volume ratio.

Identify the location of the cytosol in a eukaryotic cell and list its general functions.

Describe the three types of protein filaments that make up the cytoskeleton. Identify which underlie cilia, flagella, centrioles, the nuclear lamina, and the brush border. Tell which are readily assembled and disassembled. Tell which are involved in various cell shape changes or movements.

Explain how motor proteins interact with microtubules or actin filaments to promote cellular movement.

Describe the structure and organization of the cell nucleus. Describe the structure and function of nuclear pores.

Outline the structures and general functions of the components of the endomembrane system.

Distinguish between the rough endoplasmic reticulum and the smooth endoplasmic reticulum.

Identify three important functions of the plasma membrane.

Tell why mitochondria and chloroplasts are called semi-autonomous organelles.

Discuss the evidence for the endosymbiosis theory.

Outline the structures and general functions of mitochondria and chloroplasts.

Explain how proteins are moved via vesicles through the endomembrane system.

If you are told about the function of a specific protein, tell where and in what type of cell that protein might be found.

Sketch and label a âtypicalâ animal cell and a real animal cell such as a red blood cell or a muscle cell. Tell how it might be different than the âtypicalâ cell in terms of its organelles and shape.

Sketch and label a âtypicalâ plant cell and a real plant cell such as a root or leaf cell. Tell how it might be different than the âtypicalâ cell in terms of its organelles and shape.

Describe the fluid-mosaic model of membrane structure. Tell why membranes are described as âfluid mosaicsâ.

Draw 10 phospholipid molecules as they would be arranged in a bilayer. Label the hydrophobic and hydrophilic parts.

61. Name all the places in a cell where membranes are found.

62. Describe at least three different categories of membrane proteins and tell what they do.

63. Describe what determines how fluid membranes are.

64. Explain how lipids are synthesized at the ER membrane.

65. Explain how transmembrane proteins are inserted into the ER membrane.

66. Compare and contrast diffusion, facilitated diffusion, passive transport, and active transport.

67. Explain the process of osmosis and how it affects cell structure.

68. Outline the functional differences between channels and transporters. Compare and contrast uniporters, symporters, and antiporters.

69. Explain the difference between primary active transport and secondary active transport.

70. Describe the structure and function of the sodium-potassium pump in animal cells and a similar pump in plants and prokaryotes.

71. Describe exocytosis and endocytosis and tell what molecules are moved across the membrane by these.

Discuss membrane transport, including its function and various forms and why all membranes have each form.

73. If a given cellular process is described, tell which form of transport might be involved.

List the different categories of animal tissue, providing general functions and specific examples of each.

Name the various organ systems found in many animals, list the components of each, and describe their general functions.

bluebeaver798

Biochemistry Review Questions

What is the classification of the compound shown here?

A) an aldohexose B) a ketohexose C) an aldopentose D) a ketopentose

2. In a disaccharide, the CâO bond that joins the two rings together is called _____.

A) a hemiacetal B) a glycosidic linkage C) an alditol D) an anomer

3. What is the structure of amylopectin?

A) unbranched skeleton of glucose molecules joined by 1ï®4-ï¡-glycoside linkages

B) branched skeleton of glucose molecules joined by 1ï®4-ï¡-glycoside linkages

C) unbranched skeleton of glucose molecules joined by 1ï®4-ï¢-glycoside linkages

D) branched skeleton of glucose molecules joined by 1ï®4-ï¢-glycoside linkages

4. In a disaccharide, the CâO bond that joins the two rings together is called _____.

A) a hemiacetal B) a glycosidic linkage C) an alditol D) an anomer

5. Which type of linkage between the two rings is in the structure shown?

A) 1Â®4-b-glycoside linkage D) 1Â®1-a-glycoside linkage

B) 1Â®4-a-glycoside linkage E) 1Â®2-b-glycoside linkage

C) 1Â®1-b-glycoside linkage

6. What is the structure of cellulose?

A) unbranched skeleton of glucose molecules joined by 1Â®4-a-glycoside linkages

B) branched skeleton of glucose molecules joined by 1Â®4-a-glycoside linkages

C) unbranched skeleton of glucose molecules joined by 1Â®4-b-glycoside linkages

D) branched skeleton of glucose molecules joined by 1Â®4-b-glycoside linkages

7. Which amino acid is a basic amino acid?

A) serine B) arginine C) cysteine D) alanine E) valine

8. What monosaccharide is found in cellulose, starch, and glycogen?

A) glucose

B) galactose

C) N-acetyl-D-glucosamine

D) fructose

E) More than one of the monosaccharides above is found in cellulose, starch, and glycogen.

9. Which is not a reducing sugar?

A) glucose B) fructose C) sucrose D) galactose E) an aldopentose

10. Sucrose contains one _____ unit and one _____ unit.

11. What is the particular sequence of amino acids of a protein that are joined together by peptide bonds called?

A) the primary structure of a protein C) the tertiary structure of a protein

B) the secondary structure of a protein D) the quaternary structure of a protein

12. What is the charge on an amino acid at a pH below its pI?

A) positive

B) neutral

C) negative

D) The charge or lack of charge varies depending on the amino acid.

13. What is the C-terminal amino acid in the tetrapeptide glycylalanyisoleucylmethionine?

A) alanine B) glycine C) methionine D) isoleucine

14. How many different dipeptides can be formed when one valine reacts with one glycine?

A) 1 B) 2 C) 3 D) 4

15. What is the process of altering the shape of a protein without breaking the amide bonds that form the primary structure?

A) hydrolysis B) competitive inhibition C) denaturation D) oxidation

16. Which of the following compounds is an enzyme?

A) glucose C) N-acetyl-D-glucosamine

B) triosephosphate isomerase D) dihydrofolate

17. What is a zymogen?

A) an amino acid with a neutral charge

B) inactive precursor of an enzyme

C) a molecule that causes an enzyme to lose activity

D) a nonprotein organic molecule needed for an enzyme-catalyzed reaction to occur

18. Which of the following will the cause the rate of enzyme activity to first increase and then level off?

increasing the enzyme concentration

increasing the temperature

increasing the substrate concentration

increasing the pH

19. Which of the following make up a nucleoside?

base + sugar

base + phosphate + sugar

base + phosphate

phosphate + sugar

20. Transcription corresponds to which of the following?

the separation of the two strands of DNA to enable the formation of two identical DNA molecules

the transfer of genetic information from DNA to RNA

the transfer of genetic information from RNA to DNA

the use of genetic information to synthesize a specific protein

21. Each individual tRNA contains _____

A) a base sequence that is identical to the informational strand of DNA.

B) the sequence of codons that determines the order of amino acids in the protein.

C) an anticodon of three nucleotides that is complementary to the codon in mRNA and identifies individual amino acids.

D) an anticodon complementary to any of the three stop codons.

22. Where does energy production occur in animal cells?

A) cell membrane B) cytoplasm C) mitochondria D) nucleus

23. How many molecules of CO2 are produced for each turn of the citric acid cycle?

A) 0 B) 1 C) 2 D) 3 E) 4

25. Which is not a reaction found in stage [2] of catabolism?

A) fatty acid oxidation C) oxidative phosphorylation

B) glycolysis D) amino acid catabolism

26. What is the classification of the reaction shown?

A) oxidation D) hydrolysis

B) reduction E) isomerization

C) decarboxylation

27. Synthesis of glucose from amino acids is called

A) Glycolysis C) Gluconeogensis

B) Glycogenesis D) Hydrolysis

28. The synthesis of large molecules from smaller ones in the body is referred to as

A) catabolism C) Ketogenesis

B) anabolism D)glycolysis

29. The nucleic acid base found in the mRNA but not in DNA is

A) Adenine C) Uracil

B) Guanine D) Cytosine

30. DNA rich in A-T base pairs have

A) 1 hydrogen bond C) 2 hydrogen bonds

B) 3 hydrogen bonds D) 4 hydrogen bonds

31. Where does the energy production occur in the cell?

A) Ribosome C) Mitochondria

B) Nucleus D) Cytoplasm

32. Where does the protein synthesis occur in the cell?

A) Ribosome C) Mitochondria

B) Nucleus D) Cytoplasm

33. In the process of transcription, the flow of genetic information is from

A) DNA to DNA C) DNA to protein

B) RNA to protein D) DNA to RNA

34. Ammonium ions are converted to non-toxic nitrogen containing compounds through

A) Amino acid metabolism C) Urea cycle

B) Citric acid cycle D) transamination

35. In protein structure, B-pleated cheats are examples of

A) Primary structure C) Secondary structure

B) Tertiary structure D) Quaternary structure

36. Lactose is a disaccharide formed of

A) Glucose + fructose C) Glucose + galactose

B) Glucose + glucose D) Fructose + galactose

37. Saponification is

A) Hydrolysis of fats by strong base

B) Hydrolysis of glycerol by lipases

C) Esterification

D) Oxidation reaction

38. The connection between amino acid residues in molecules of protein is

A) glycosidic linkage C) peptide linakge

C) ether linkage D) phosphodiester linkage

39. Polyunsaturated fatty acids are generally

A) Oil at room temperature C) Solid at room temperature

B) Semisolid at room temperature D) All of the above

40. Maximum energy is produced by

A) Carbohydrates C) Lipids

B) Proteins D) Nucleic acids

41. A polynucleotide contains _____

A) one free phosphate group at the 5' end.

B) a backbone of alternating sugar and base groups.

C) one free phosphate group at the 1' end.

D) one free OH group at the 5' end.

42. How many molecules of CO2 are produced for each turn of the citric acid cycle?

A) 0 B) 1 C) 2 D) 3 E) 4

43. How many molecules of GTP are produced for each turn of the citric acid cycle?

A) 0 B) 1 C) 2 D) 3 E) 4

44. Which is the enzyme that hydrolyzes triacylglycerols?

A) acetyl CoA D) lipase

B) protease pepsin E) succinate dehydrogenase

C) amylase

BIOCHEM 423 Chapter Notes - Chapter 11.1: Anabolism, Organic Compound, Catabolism

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