1. What are the rate-limiting enzymes of the Krebs cycle?

Citrate synthase, isocitrate dehydrogenase, alpha- ketoglutarate dehydrogenase

And which molecules are formed in this cycle and included in the electron transport chain?

NADH and FADH

2. Which enzyme is required for the formation of the molecule produced to enter the Krebs cycle at the end of the
glycolysis pathway?

Pyruvate dehydrogenase

What constitutes the content of this enzyme?

Thiaminepyrophosphate (TPP)
CoA
FAD + and NAD +
Lipoic acid

3. What are the functions of gluconeogenesis, glycolysis, glycogenolysis, glycogenesis, krebs cycle, pentose
phosphate pathway, Urea cycle, Glucuronic acid pathway?

Gluconeogenesis: synthesis of glucose from non-carbohydrate sources

Glycolysis: breakdown of glucose into pyruvate, generating ATP and NADH

Glycogenolysis: breakdown of glycogen to release glucose.

Glycogenesis: synthesis of glycogen from glucose.

Krebs Cycle: oxidation of acetyl-CoA to CO₂ and H₂O, generating NADH, FADH₂, and ATP

Pentose Phosphate Pathway: Ensuring NADPH production, effective in antioxidant system, for formation of pentose sugar

Urea Cycle: conversion of ammonia to urea for excretion.

Glucuronic Acid Pathway: detoxification and participate in the synthesis of glycosaminoglycan

What are the rate- limiting enzymes of these pathways? In what situation are these pathways activated?

Gluconeogenesis: Fructose-1,6-bisphosphatase.

Glycolysis: Phosphofructokinase-1 (PFK-1).

Glycogenolysis: Glycogen phosphorylase.

Glycogenesis: Glycogen synthase

Krebs Cycle: Citrate synthase, isocitrate dehydrogenase, α-ketoglutarate dehydrogenase

Pentose Phosphate Pathway: Glucose-6-phosphate dehydrogenase

Urea Cycle: Carbamoyl phosphate synthetase I.

Glucuronic Acid Pathway: UDP-glucuronosyltransferase.

What kind of diseases do defects in the enzymes of these pathways cause?

 4. What are the precursor molecules required for gluconeogenesis?

Lactate, glycerol amino acids, propionate

5. What are glycogen storage diseases and causes?

Von Gierke’s disease – glucose 6 phosphate deficiency

Myophosphorylase deficiency. – muscle phosphorylase deficiency, but liver is normal
Pompes disease lusosomal alpha 1 – 4 glycosidase deficiency
↑

Limit dextrinosis. - branching enzyme deficiency

Mc Ardle’s disease. – muscle phosphorylase deficiency, but liver is normal

6. Which element is necessary for the absorption of glucose and amino acids in the small intestines?

Na+ and GLUT2

7. What is the most important pathway for erythrocytes?

Glycolysis

Why is this pathway important?

Glycolysis is essential for producing ATP

8. How is metabolic control of glucose achieved?

1) Insulin is released when blood glucose is high to decrease the blood glucose, glucose is converted to glycogen

2) glucagon is released when blood glucose is low and uses the stored glucose in the liver to increase the blood glucose

9.What is diabetic ketoacidosis? Why does it occur?

a serious complication of diabetes, occurring due to insufficient insulin

10. What are the general properties of lipids?

D Heterogeneous group
Consist mainly of carbon and hydrogen
They are insoluble in water, but soluble in non-polar solvents
It is important that they are taken with diet.
 11. How are lipids classified?

1-According to their structure

2-According to their functions

How many types of lipid classifications are there?

What are these classifications?

1 - Simple Lipids -> Fatty acids, triglycerides, waxes

2- Complex lipids -> Phospholipids, Glycolipids, Lipoproteins
3- Isoprene Derived lipids -> Terpenes and steroids

12. What are lipoproteins?

They are molecular complexes consisting of lipids and proteins.

What are the functions of lipoproteins, their contents, where they are synthesized, and their precursors?

Function -> transport vehicles for lipids in blood plasma.

Contents -> HDL LDL ILD VLDL CM
Synthesized in -> liver and intestine

13. What is the general mechanism of cholesterol-lowering drugs? Which enzyme is it associated with?

Statins are drugs that lower cholesterol by inhibiting HMG-CoA reductase.

14. What are the functions and properties of molecules synthesized from arachidonic acid?

P Eicosanoids -> derived from arachidonic acid, serve as signaling molecules that regulate inflammation,
blood clotting, and immune responses. They function locally, influencing nearby cells and modulating
various physiological processes.

15.What methods are used for total lipid determination?

& Phosphovanilin method was used for the determination of total plasma lipid.
*16. What methods are used to determine cholesterol? Enzymatic assays colorimetric tests

17. What methods are used for protein determination? Biuret method

18. Which receptors are used in the hormone mechanism?

• In or on the surface of the cell membrane (for protein, peptide, catecholamine hormones)
• In the cell cytoplasm (steroid hormones)
• In the cell nucleus (receptors for the thyroid hormones)

What are the properties of these receptors?

How are these receptors classified?

19. What is the general name of the molecules used for hormones to act within the cell and what are the
-

names of these molecules?

Hormone-receptor complexes

D 20. What are the general characteristics of hormones?

Chemical messengers, regulate physiological processes

& 21. From which macromolecule are steroid hormones synthesized?

Cholesterol

*Examples of steroid hormones?

cortisol, aldosterone, estrogen

22. What is a peptide bond?

. It is the covalent bond formed between the carbon of the carboxyl group of the first amino acid and the
nitrogen of the amine group of the second amino acid.

What are the properties of the peptide bond?

partial double bond character, shorter than a single bond, rigid and planar, is covalent bond.

What happens to the peptide bond in case of denaturation?

Denaturating agents destroy secondary and tertiary structures, without affecting the primary structure.
 23. What are the functions of vitamins?

Vitamin A- visual function B1: support energy metabolism Vitamin

E- prevents oxidation of LDL B2: active forms FMN and FAD
K- effective in coagulation. B3: effective as a coenzyme
D- increase the uptake and retention of calcium B9: effective in the development of the fetus in the
Vitamin C- synthesis of collagen first weeks of pregnancy
24. Classification of vitamins

1. Water soluble.
2. Lipid soluble.

25. What are the systemic names of vitamins?

• Vitamin B1 (Thiamine) • Vitamin B6 (Pyridoxine)

• Vitamin B2 (Riboflavin) • Vitamin B7 (Biotin)
• Vitamin B3(Niacin) • Vitamin B9 (Folic acid)
• Vitamin B5 (Pantothenic acid) • Vitamin B12 (Cobalamin)
• Vitamin C (Ascorbic acid) #

26. What diseases occur in vitamin deficiencies

B1 - beriberi& wernickle
B2 - cracks on the corner of the mouth
B3 - pellagra, dermatitis, diarrhea, dementia
B5 - deficiency is rare
DB6 - no hemoglobin protein
B12 - anemia
& C - scorbute

27. Which vitamins are synthesized endogenously?

K D B3 B7

28. How is the peptide bond calculated given the number of amino acids in a polypeptide chain?

-1

29. How to calculate the number of aminoacids in a polypeptide chain with a known number of peptide bonds?

+1
* 30. What are antioxidant molecules? (enzymatic-non-enzymatic)

enzymatic antioxidants Vitamin D, K, B, and sodium

non-enzymatic antioxidants Vitamin C

31. What are the general properties of enzymes? What is the working principle of enzymes?

They’re biologically sourced catalysts.

They’re special catalysts

They’re not passive

32.What are the factors that affect the activity of enzymes?

Temperature, pH, enzyme and substrate concentration

A 33. What are the specific terms related to enzymes?

Holoenzyme consists of apoenzyme and coenzyme

Enzymes that catalyze the same reaction but differ in structure are called isoenzymes
Allosteric enzymes give a sigmoidal graph

34. Which metabolic pathway occurs in which cell compartment? (For all pathways...)

P 35. What is the tripeptide that is effective in the antioxidant system and what is its structure?
Glutathione is composed of glutamate, cysteine, and glycine

36.What are the structure and functions of hemoglobin and collagen?

Hemoglobin provides to transport oxygen from the lungs to the peripheral tissues.
Hemoglobin provides to transport carbon dioxide from the tissues to the lungs.
Collagen is the most abundant protein in the human body.
Collagen is rich in the proline and glycine.
The kinks in the collagen structure occur with proline

37. What is the importance of the amino acid glycine?

It is an important precursor that is glycine for purines and Heme synthesis begins with glycine and succinyl
CoA.

&What is the main feature of glycine ?

It is found in the structure of hemoglobin

It is the precursor of porphyrin structure.
It takes part in the formation of the purine ring.

What is its structure?

Smallest amino acid

What is its difference from other amino acids?

P38. What are the factors necessary for the stabilization of proteins?
hydrogen bonds, ionic interactions, hydrophobic effect

& 39. What is the importance, function, and rate-limiting enzyme of heme synthesis?
Heme synthesis occurs in mitochondria and cytoplasm.
Hemoglobin synthesis occurs in bone marrow and liver.
All reactions in heme synthesis are irreversible.
The importance of heme synthesis is that it produces hemoglobin that transport oxygen from lungs to the
peripheral tissues and transport CO2 from tissues to lungs. It also forms other enzymes: catalase, myoglobin,
peroxidase, and cytochrome.

40. What are purine and pyrimidine?

Purines -> adenine and guanine

Pyrimidine -> thymine cytosine uracil

What do their structures contain?

Purine -> double ring structure

Pyrimidine -> six membrane ring

What are the connections in its content? Hydrogen bond

41. What is a buffer? A solution that resists changes in pH.

& What is its function in living systems? Maintains pH stability

42. Define what pH is. measure of the acidity

What is body pH? 7

What happens to the H ion concentration if the pH increases?

9)1[

Low H ion = high pH = basic solution

What happens to the H ion concentration if the pH decreases?

High H ion = low pH = acidic solution

What does pH change cause in living systems? Structural proteins undergo changes and Enzymes lose their
activity
43. What are the methods we use in practice?
2 IDK what practice or

3
What is determined using these methods?
experiment she’s talking abt
What are the calculations used in these methods?

What is the name of the device used in these methods?

44. What are the pathways/reactions used to remove ammonia from the body?

Transamination, deamination, urea cycle

45. What is active transport and passive transport?

Active -> From low concentration to high concentration (requires ATP)

Passive -> from high concentration to low concentration ( no ATP)

Which transport systems are active and which are passive?

Passive -> simple diffusion, facilitated diffusion

Active -> Na/K pump

46. What are the diseases caused by purine and pyrimidine metabolism defects?

Purine -> gout, lesch-Nyhan syndrome, adenosine deaminase deficiency, hypouricemia

Pyrimidine -> orothidylate decarboxylase