MICROBtruru4u47474u4u4u44uy5uruhrIO.pptx

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1. ENZYMOLOGY:- PRESENTING MY LEARNINGS ON THE TOPICS LIKE: APOENZYME,COENZYME,PROSTHETHIC GROUPS . NAME: DRASHTI PANCHAL .P. SUBJECT: BIO-CHEMISTRY SUBMITTING TO: MS. KRISHNA

2. OUTLINES:- INTRODUCTION TO ENZYME TERMS APOENZYMES AND HOLOENZYMES INTRODUCTION TO COENZYMES INTRODUCTION TO PROSTHETHIC GROUPS CONCLUSION

3. INTRODUCTION:- WHAT IS ENZYME ? DEFINITION:- Enzymes are protienitious biocatalyst (except ribozyme) which work by lowering the activation energy and remain unchanged after reaction . 1. Enzymes are found in all living cells. 2. Enzymes are made of protein. 3. Enzymes are Biological Catalysts. 4. Enzymes speed up reactions. 5. Enzymes are unchanged by the reaction. 6. A catalyst is a substance that starts or speeds up a chemical reaction.- It lowers the activation energy required for the reaction to take place. 7. Enzymes are used by cells to trigger and control chemical reactions.* Without enzymes, several reactions in cells would never occur or happen too slowly to be useful.

4. FISCHER’S LOCK AND KEY MODEL: Model is proposed by Emil Fischer .The substrate can fit into its complementary site on the enzyme as a key fits into a lock .Two shapes are rigid and fixed. Perfectly complement each other.

5. TERMS:- APOENZYMES COFACTOR HOLOENZYME PROSTHETHIC GROUP Apoenzymes, coenzymes, and prosthetic groups are essential components of enzymes that facilitate biochemical reactions Understandling their roles enhances our grasp of metabolic pathways and enzyme functionality. This presentation will explore their definitions, functions, and significance in biochemistry

6. Apoenzyme and holoenzyme:- The enzyme without its non protein moiety is termed as apoenzyme and it is inactive. Holoenzyme is an active enzyme with its non protein component. If the nonprotein part is a metal ion such as Zn 2+ or Fe2+, it is called a cofactor. * If it is a small organic molecule, it is termed a coenzyme.

7. COENZYME- INTRODUCTION An enzyme is a protein that functions as a catalyst to mediate and a speed chemical reaction. Coenzyme is a substance that enhances the action of an enzyme. The catalytic activity of enzymes mostly depends on the presence of non-protein compounds called coenzymes. coenzymes cannot be isolated from apoenzymes without denaturation of the enzyme proteins They cannot by themselves catalyze a reaction but they can help enzymes to do so. In technical terms, coenzymes are organic nonprotein molecules that bind with the protein molecule (apoenzyme) to form the active enzyme (holoenzyme). A number of the water-soluble vitamins such as vitamins B1, B2 and B6 serve as coenzymes.

8. Coenzyme – definition Coenzyme (Biology definition) : Molecule required by a particular enzyme to carry out catalysis of a chemical reaction is called as coenzyme. Coenzymes are small organic molecules that transport chemical groups in an enzymatic reaction OR Any of a number of freely diffusing organic compounds that function as cofactors with enzymes in promoting a variety of metabolic reactions. Some of these chemicals such as riboflavin, thiamine and folic acid are vitamins, (acquired) Example of coenzyme ;. nicotineamideadenine dinucleotide (NAD), Nicotinemide adenine dinucelotide phosphat e (NADP), flavin adenine dinucleotide (FAD). These three coenzymes are involved in oxidation or hydrogen transfer. .

9. COENZYME- FUNCTIONS:- The coenzyme is essential for the biological activity of the enzyme. A coenzyme is a low molecular weight organic substance, without which the enzyme cannot exhibit any reaction. A coenzymes prepares the active site for catalytic activity. The function of coenzyme is to transfer of groups between enzymes. A coenzyme is necessary helper for enzymes that assist in biochemical transformations. A coenzyme transport a variety of chemical groups (such as Hydride, Acetyl, Formyl, Methenyl , Methyl)

10. PROSTHETHIC GROUPS- INTRODUCTION:- Prosthetic group is present in enzymes and non- enzyme proteins. Prosthetic group is always tightly attached to the proteinous part of an enzyme,Prosthetic group mainly participate in Redox reactions. Example is heme , a prosthetic group present in cytochrome oxidase. Tightly integrated into the enzyme structure by covalent or non- covalent forces. Prosthetic groups are non-peptide substances that bind tightly together. Non-peptides (non-proteins) in prosthetic groups bind to other proteins and assist them in a variety of ways. A protein that is bonded to a prosthetic group is known as a holoprotein

11. CONTD.. a ) ORGANIC: Attach permanently to enzymes. EG:- HB contains haem [iron] and it is bound to protein Haem enables HB to carry oxygen Pyridoxal phosphate Flavin mononucleotide(FMN) Flavin adenine dinucleotide (FAD) Thiamin pyrophosphate (TPP) Biotin. B) IN-ORGANIC Inorganic Metals are the most common prosthetic groups. Metal ions - Co, Cu, Mg, Mn, Zn. Fe.

12. CONCLUSION:- In conclusion, apoenzymes, coenzymes, and prosthetic groups are integral to enzymatic function. A deeper understanding of these components can lead to advancements in biochemistry and medicine.