DOC-20240227-WA0015..pptx action presentation

Mechanism of enzyme action presentation ppt
This is the very easy and convenient presentation for the mechanism of enzyme action and letting the kinetics of enzyme action

1. BIOCHEMISTRY P RESEN T A T I ON

2. GROUP MEMBERS ✦ MASHAL ZAHRA ✦ MAHAM NAEEM ✦ MOAZMA YOUSAF ✦ SHAHRBANO ✦ MAHNOOR SUBMITTED TO ✦ Dr. ASAD ALI ARIF

3. ✦ CHEMISTRY OF PROTEIN & AMINO ACIDS. ✦ C H E M I S T R Y O F HORMONES. TOPIC NAME

4. AMINO ACIDS ✦ Amino acid is an organic compound that contains both an amino (-NH2) and carboxylic acid (-COOH) functional group. ✦ They are basic building blocks of proteins, and they serve as the nitrogenous backbones for compounds like neurotransmitters and hormones.

5. PEPTIDE BOND FORMATION ✦ Amino acids link together through peptide bonds to form proteins. ✦ The peptide bond is formed through a condensation reaction, where the amino group of one amino acid reacts with the carboxyl group of another, releasing water in the process.

6. CLASSIFICATION OF AMINO ACIDS Essential Amino Acids ✦ These amino acids cannot be synthesized by the human body in sufficient amounts or at all. ✦ It is essential to obtain them through dietary sources. Non-Essential Amino Acids ✦ The human body can synthesize these amino acids in sufficient quantities, so it is not essential to obtain them directly from the diet.

7. Semi-Essential or Conditionally Essential Amino Acids ✦ These amino acids are generally considered non-essential because the body can synthesize them under normal conditions. ✦ However, under certain circumstances (e.g., illness, stress, growth stages), the body may not produce enough of these amino acids, and they may need to be obtained from the diet. Special Amino Acids(Non-protein forming) ✦ These amino acids are produced in our body but do not take part in protein synthesis.

8. ESSENTIAL ✦ Lysine ✦ Tryptophan ✦ Phenylalanine ✦ Methionine ✦ Threonine ✦ Leucine ✦ Isoleucine ✦ Valine Non-essential ✦ Hydroxyproline ✦ Histidine ✦ Cysteine ✦ Proline ✦ Alanine ✦ Aspartic acid ✦ Glutamic acid Semi-essential ✦ Arginine ✦ Tyrosine ✦ Cystine ✦ Glycine ✦ Serine Special ✦ Citrulline ✦ Ornithine ✦ Taurine ✦ DOPA ✦ GABA

9. REACTIONS OF AMINO ACIDS Reactions due to amino group i) Oxidative deamination ✦ An amino group is removed and corresponding a-keto acid is formed. ✦ α-keto acid produced is either converted to glucose or ketone bodies or is completely oxidized.

10. ii) Transamination ✦ Transfer of an a amino group from an amino acid to an a keto acid to form a new amino acid and a corresponding keto acid. iii) Formation of carbamino compound ✦ CO2 binds to a amino acid on the globin chain of hemoglobin to form carbamino hemoglobin.

11. Reactions due to carboxyl group Decarboxylation ✦ Amino acids undergo alpha decarboxylation to form corresponding amines. Formation of amide linkage ✦ Non a carboxyl group of an acidic amino acid reacts with ammonia by condensation reaction to form corresponding amides

12. Reactions due to both amino & carboxyl groups i) Formation of peptide bond ✦ Carboxyl group of an amino acid binds with amino group of another amino acid forming a peptide bond with the loss of one molecule of water.

13. Reactions due to side chains i) Ester formation ✦ OH containing amino acids e.g. serine, threonine can form esters with phosphoric acid in the formation of phosphoproteins (figure-1). ✦ OH group containing amino acid can also form: Glycosides - by forming O- glycosidic bond with carbohydrate residues (figure-2).

14. ii) Formation of sulphide bonds ✦ Cysteine has a sulfhydryl group(SH) group and can form a disulphide (S-S) bond with another cysteine residue. ✦ The dimer is called Cystine.

15. iii) Formation of disulphide bond ✦ Two cysteine residues can connect two polypeptide chains by the formation of interchain disulphide chains.

16. PROTEINS ✦ Proteins are polypeptide structures consisting of one or more long chains of amino acid residues. ✦ They carry out a wide variety of organism functions, including DNA replication, transporting molecules, catalyzing metabolic reactions, and providing structural support to cells.

17. PROTEIN STRUCTURES PRIMARY STRUCTURE ✦ Primary structure of a protein is defined as the sequence of amino acids linked together to form a polypeptide chain. ✦ Primary structure refers to the linear arrangement of amino acids in a protein. ✦ Peptide bonds connect amino acids, forming the primary structure of the protein.

18. SECONDARY STRUCTURE ✦ The most common types of secondary structures are the α helix and the β pleated sheet. Alpha Helices ✦ Secondary structure formed by coiled polypeptide chains. Beta Sheets Secondary structure characterized by intermolecular hydrogen bonding.

19. TERTIARY STRUCTURE ✦ The tertiary structure of a protein refers to the overall three-dimensional arrangement of its polypeptide chain in space. ✦ The bonds in the tertiary structure of a protein involve disulfide bonds, hydrogen bonds, ionic bonds, and hydrophobic interactions.

20. QUATERNARY STRUCTURE ✦ The quaternary structure of a protein is the association of several protein chains or subunits into a closely packed arrangement. ✦ Each of the subunits has its own primary, secondary, and tertiary structure. ✦ Quaternary structure exists in proteins consisting of two or more identical or different polypeptide chains (subunits).

21. CLASSIFICATION O F PROTEINS

22. FUNCTIONS OF PROTEINS ✦ Enzymatic Catalysis: Proteins act as catalysts, speeding up biochemical reactions in cells. ✦ Hormonal Regulation: Hormonal proteins, like insulin, regulate various physiological processes and maintain homeostasis. ✦ Immune Defense: Antibodies, a type of protein, play a key role in recognizing and neutralizing foreign invaders in the immune system.

23. ✦ Cellular Communication: Signaling proteins transmit messages within and between cells, regulating growth, development, and responses to external stimuli. ✦ Transport: Specialized proteins like hemoglobin transport molecules, such as oxygen and nutrients, throughout the body. ✦ Structural Support: Proteins provide the framework for cells, tissues, and organs, maintaining their integrity.

24. HORMONES ✦ The English physician E. H. Starling discovered in collaboration with the physiologist W. M. Bayliss secretin, the first hormone, in 1902. ✦ Hormones are chemicals that coordinate different functions in your body by carrying messages through your blood to your organs, skin, muscles and other tissues. ✦ These signals tell your body what to do and when to do it.

25. GROWTH HORMONES ✦ Human growth hormone is a hormone of the anterior pituitary gland and is also known as somatotropin or somatotropic hormone (STH). ✦ Its basic function is to cause body cells to grow.

26. OXYTOCIN ✦ This is a hormone of the posterior pituitary gland. ✦ It stimulates contraction of the smooth muscles of the pregnant uterus. ✦ It is released in large quantities just prior to delivery. ✦ It causes increase milk ejection in lactating breasts. ✦ In large doses oxytocin causes vasodilatations and decreases blood pressure. ✦ It accelerates transport of the seminal fluid towards the fallopian tubes, favoring fertilization.

27. IN S U L IN ✦ Insulin is a small protein which acts to lower the blood glucose level. ✦ This hormone is secreted by beta cells of the islets of Langerhans of the pancreas. ✦ Insulin is small soluble protein containing 51 aminoacids. ✦ It promotes translation of mRNA in ribosomes to form new proteins. ✦ Insulin is essential for growth, as it increases protein formation. ✦ It increases utilization of glucose for energy.

28. APPLICATIONS IN PHARMACY ✦ Corticosteroid Creams: Topical application for anti-inflammatory effects on the skin, treating conditions like eczema and psoriasis. ✦ Insulin Therapy: Manages diabetes by regulating blood glucose levels through insulin injections or analogs. ✦ Contraceptives: Regulate reproductive hormones to prevent unwanted pregnancies, commonly through estrogen and progesterone combinations. ✦ Glucocorticoid Therapy: Suppresses inflammation and immune responses, used in conditions like asthma and rheumatoid arthritis.