GPAT.pptx introduction biochemistry and it's terms

Gpat ppt

1. Carbohydrates Carbohydrates may defined as polyhydroxy aldehyde or ketone or compounds which Produce them on hydrolysis . Functions: 1)They are most abundant dietary source of energy (4 kcal/g) for all organisms. 2)Carbohydrates are precursors for many organic compounds (fats, amino acids). 3)They participate in structure of cell membrane & cellular function such as Cell growth,fertilization . 4)Carbohydrates are structural components of many organisms. 5)They serves as storage form of energy to meet immediate energy demands of body. 6)Carbohydrates utilized as raw material for several industries. Ex-paper, plastics, textiles, alcohol etc.

2. Classification of Carbohydrates

3. Reducing Sugar Non Reducing Sugar Carbohydrate with free aldehyde and ketone group free aldehyde and ketone group are not available In hemiacetal and hemiketal form In acetal and ketal form Shows mutarotation Not Shows mutarotation Form osazone with Phenyl hydrazine Do not Form osazone Reduce cupric ion of CUSO 4 Do not Reduce cupric ion of CUSO 4 Examples – Glucose, Fructose, Maltose, Lactose Examples – Sucrose, Trehalose . Starch

4. If two monosaccharides differ form each other in their configuration around single specific carbon atom, they are referred as epimer to each other. Eg - Glucose & Galactose are epimer with regard to carbon 4 (C4 – epimers ) i.e . They differ in arrangement of -OH group at C4 The interconversion of epimers Eg - Glucose to galactose & galactose to glucose is known as epimerization & a group of enzymes namely epimerase catalyse this reaction Epimer

5. α-D-glucose β-D-glucose Anomer The α & β cyclic forms of D-glucose are known as anomers . They differ from each other in configuration only around C1 known as anomeric carbon ( hemiacetal Carbon). In α anomer -OH group → on anomeric carbon → to the opposite side of -CH2OH of sugar ring. β anomer . -OH group → on anomeric carbon → to the Same side of -CH₂CH of sugar ring.   The anomers differ in certain physical & chemical properties

6. The α & β anomers of glucose have different optical rotations. The specific optical rotation of freshly prepared glucose (α- anomes ) solution in water is +112. 2° which changes & attain equilibrium with constant value of +52.7°. In presence of alkali decrease in optical rotation is rapid , optical rotation of β-glucose is +18.7°. Mutarotation is defind as change in specific optical rotation representing interconversion of α & β form of D-glucose to an equilibrium mixture α-D-glucose (36%) 1% β-D-glucose (63%) α-D-glucose ⇌ Equilibrium mixture ⇌ β-D-glucose Mutarotation

7. Major pathways:- Glycolysis:- oxidation of glucose to pyruvate & lactate Citric acid cycle – oxidation of acetyl CoA To CO 2 . Glyconeogenesis - synthesis of glucose form non carbohydrate precursor Glycogenesis - Formation of glycogen from glucose Glycogenolysis - Breakdown of glycogen to glucose and then to lactate and pyruvate Hexose monophosphate shunt - Glucose is directly oxidized to CO 2 and H 2 O Uronic acid pathway – Glucose is converted to glucaronic acid and pentose Metabolism

8. Glycolysis

9. TCA Cycle / Citric Acid Cycle/ Kreb cycle

10. Reductometric method Enzymatic method Nelson Somogyi method 1.Hexokinase method Folin wu method 2.Glucose oxidase peroxidase method O - Toludine method 3. Used in dry analysis like glucometer Identification tests Molisch test, Fehlings test, Benedicts test, Tommers test, Barfoeds test, Seliwanofs test, Osazone test. Iodine test Methods for estimation of glucose

11. Diabetes Mellitus Type I – Insulin dependant or juvenile onset diabetes Type II – Non insulin dependant or Adult onset diabetes Lactose Intolerance - Lactate dehydrogenase Fructose Intolerance – Aldolase Galactosaemia – Galactokinase , UDP galactose epimerase , Galactose -1- Phospahate uridyl transferase Disease associated with carbohydrate metabolism

12. Type Name Enzyme defect Organ(s) Involved Characteristic features I von Gierke's disease (type I glycogenosis ) Glucose-6-phosphatase Liver, kidney and intestine Glycogen accumulates in hepatocytes and renal cells, enlarged liver and kidney, fasting hypoglycemia , lactic acidemia ; hyperlipidemia ; ketosis; gouty arthritis. II Pompe's disease Lysosomal α-1,4 glucosidase (acid maltase) All organs Glycogen accumulates in lysosomes in almost all the tissues; heart is mostly involved; enlarged liver and heart, nervous system is also affected; death occurs at an early age due to heart failure.

13. III Cori's disease (Limit dextrinosis, Forbe's disease) Amylo α-1,6 gluscosidase (debranching enzyme) Liver, muscle, heart , leucocyte Branched chain glycogen accumulates; liver enlarged; clinical manifestations are similar but milder compared to von Gierke's disease. IV Anderson's disease (amylopectinosis) Glucosyl 4-6 transferase ( Branching enzyme) Most tissue A rare disease, glycogen with only few branches accumulate; cirrhosis of liver, impairment in liver function. v McArdle's disease (type V glycogenosis) Muscle glycogen phosphorylase Skeletal muscle Muscle glycogen stores very high, not available during exercise; subjects cannot perform strenous exercise; suffer from muscle cramps; blood lactate and pyruvate do not increase after exercise; muscles may get damaged due to inadequate energy supply. VI Her's disease Liver glycogen phosphorylase Liver Liver enlarged; liver glycogen cannot form glucose (pyruvate and lactate can be precursors for glucose); mild hypoglycemia and ketosis seen, not a very serious disease. VII Tarui's disease Phosphofructokinase Skeletal muscle , erythrocytes Muscle cramps due to exercise; blood lactate not elevated; hemolysis occurs.

14. Amino acids L amino acids All are optically active except glycine Carries same no. of positive and negative charge i.e. no net charge and exist as zwitter ion Classification of amino acids Proteins and amino acids

15. Nutritional Requirement Essential Amino acid Non-Essential Amino Acid Semi Essential Amino Acid Arginine Alanine Arginine Valine Aspartic Acid Histidine Histidine Asparagine Isoleucine Glutamate Leucine Glutamine Lysine Glycine Methionine Cysteine Phenylalanine Serine Threonine Tyrosine Tryptophan Proline Amino acid classification based on their metabolic Fate. Glycogenic amino acids – Ketogenic amino acids - leucine and lysine Glycogenic and ketogenic amino acids - isoleucine, phenyl- alanine, tryptophan, tyrosine

16. polymers of L-α-amino acids . 4 levels of organization : Primary structure : The linear sequence of amino acids forming the backbone of proteins (polypeptides). Secondary structure : The special arrangement of protein by twisting of the polypeptide chain. Tertiary structure : The three dimensional structure of a functional protein. Quaternary structure : Some of the proteins are composed of two or more polypeptide chains referred to as subunits. The special arrangement of these subunits is known as quaternary structure. The term protein Is generally used for a polypeptide containing more than 50 amino acids. Proteins

17. Edmans reagent - Determination structure of protein: Primary structure

18. Sangers reagent -

19. identified by treatment of protein with dansyl chloride. It binds with N-terminal amino acids to form dansyl polypeptides. These polypeptides on hydrolysis yield N-terminal dansyl amino acid. The number of dansyl amino acids produced is equal to number of polypeptide chains in a protein . Enzymatic cleavage: The proteolytic enzymes such as trypsin, chymotrypsin, pepsin and elastase exhibit specificity in cleaving the peptide bonds . 3.Determination of amino acid sequence Sequentor Secondary ,tertiary and quaternary structure X – ray crystallography and NMR 2.Number of polypeptides