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Biochemistry 저자: Mind Map: Biochemistry

1. Importance of non polar amino acids

1.1. three dimensional strucutre due to hydrophobic interactions

1.2. Sickle cell anemia (replacement of 6th amino acid glutamate with valine at beta hemoglobin A)

2. Importance of polar amino acids

2.1. Hydrogen bond

2.2. SH of cysteine in enzyme active site

2.3. Disulfide to stabilize ex: albumin- insulin-imminoglobulins

3. Semi essential

4. Types of bonds in protein

4.1. Covalent

4.1.1. Amide bond

4.1.2. Di sulfide bond

4.2. non covalent

4.2.1. Hydrophobic interactions

4.2.2. Hydrogen bond

4.2.3. Electostatic interactions (ionic)

5. Conformation of protein

5.1. Primary

5.2. secondary

5.3. tertiary

5.4. quaternary

6. Shape of protein

6.1. Fibrous

6.2. Globular

7. enzymes classification according to reaction

7.1. Oxidoreductases

7.1.1. Oxidases

7.1.2. Hydroperoxidases

7.1.2.1. Catalase

7.1.2.2. G-SH Peroxidase

7.1.3. Dehydrogenases

7.1.3.1. NAD,NADP-dependent --> Lactate dehydrogenase

7.1.3.2. FMN,FAD-dependent --> Saccinate dehydrogenase

7.1.4. Oxygenases

7.1.4.1. Dioxygenase

7.1.4.2. Monooxygenase

7.1.5. Reductases

7.2. Transferrases

7.2.1. Aminotransferase

7.2.2. Transasylace

7.2.3. Transmethylase

7.3. Hydrolases

7.3.1. Esterases

7.3.2. Peptidases

7.3.3. Phosphatases

7.4. Lyases

7.4.1. Decarboxylases

7.4.2. Hydratases

7.4.3. Dehydratases

7.5. Isomerases

7.5.1. Racemases

7.5.2. Epimerases

7.5.3. Mutases

7.6. Ligases

7.6.1. Syntheatases

7.6.2. Carboxylases

8. Co factors

8.1. essential ions

8.1.1. Metal activating enzymes

8.1.2. Metalloenzymes

8.1.2.1. Carbonic anhydranse --> zn metalloenzymes

8.2. Co enzymes

8.2.1. co susbtrate

8.2.1.1. NADH.ATP

8.2.2. prothetic group

8.2.2.1. Flavin Adenine Dinucleotide

9. Metabolite enzymes

9.1. ATP

10. vitamin or vitamine dervied enzymes

11. enzyme specifity

11.1. Absolute

11.2. Relative

11.3. Group

11.4. Stereochemical

12. Regulation of enzymes

12.1. (Activity regulation) Short term - rapid - qualitative

12.1.1. induction

12.1.2. Repression

12.1.3. Degradation

12.2. (Amount regulation) Long term - slow - quantitative

12.2.1. Allosteric regulation

12.2.2. Feedback regulation

12.2.3. Covalent modification

12.2.3.1. Phoshorylation

12.2.4. Activation by cleavage

12.3. Compartmentation

13. Organic catalysts

13.1. Ribozymes

13.2. Enzymes

13.2.1. Simple protein enzymes

13.2.2. Conjugated protein enzymes (Holoenzymes)

13.2.2.1. Proteiin part

13.2.2.2. Non protein part

13.2.2.2.1. Co factors

14. Activators

14.1. allosteric regulation

14.1.1. AMP for phosphofructokinase 1 enzymes

14.2. Covalent modification

14.2.1. Phosphorylation

14.3. Pepetide cleavage

14.4. Keep -SH active by cofactors

14.4.1. Vitamin C for glyceraldehyde 3 P dehydrogenase enzymes

14.5. Ions as cofactors

14.5.1. Mg++ for kinases

15. Protein

15.1. Amino Acids

15.1.1. Primary Amino Acids

15.1.1.1. Polar

15.1.1.1.1. Nuetral

15.1.1.1.2. Acidic

15.1.1.1.3. Basic

15.1.1.2. non polar

15.1.1.2.1. Neutral

15.1.2. Derived Amino Acids

15.1.2.1. 4 hydroxyproline

15.1.2.2. 5 hydroxy lysine

15.1.2.3. cystine

15.1.3. Non protein Amino Acids

15.1.3.1. Beta Alanine

15.1.3.2. GABA

15.1.3.3. Dopa

15.1.3.4. Diiodotyrosine

15.2. Proteins

15.2.1. simple

15.2.1.1. protamines

15.2.1.2. histones

15.2.1.3. scleroproteins

15.2.2. Compound or conjugated

15.2.2.1. phosphoproteins

15.2.2.2. lipoproteins

15.2.2.3. glycoproteins

15.2.2.4. nucleoproteins

15.2.2.5. chromoproteins

15.2.2.6. metalloproteins

15.2.3. Derived

15.3. Peptides

15.3.1. L carnosine

15.3.2. Glutathione

15.3.3. Many hormones

16. Inhibitors

16.1. reversible

16.1.1. Competitive

16.1.2. Non competitive

16.2. Irreversible

16.2.1. Example: Iodoacetate reacts with -SH of glyceraldehyde 3 P dehydrogenase enzymes

17. Monosaccharide

17.1. Function group

17.1.1. Aldose

17.1.2. Ketose

17.2. Number of Carbon atoms

17.2.1. Triose

17.2.2. Pentose

17.2.3. Hexose

18. Isomers

18.1. D,L

18.2. a,B

18.3. Epimers

18.4. Aldose,Ketose

19. Disaccharide

19.1. Maltose

19.1.1. 2 D glucose -- a 1,4 glucosidic bond

19.2. Lactose

19.2.1. Galactose and glucose -- B 1,4 galactosidic bond

19.3. Sucrose

19.3.1. Fructose and glucose -- b 2,1 fructosidic bond

20. Polysaccharide

20.1. Homogenous

20.1.1. Glucosan

20.1.1.1. Starch

20.1.1.2. Glycogen

20.1.1.3. Cellulose

20.1.2. Fructosan

20.1.2.1. Inulin

20.2. Heterogenous

20.2.1. Neutral

20.2.2. Acidic (GAGs)

20.2.2.1. Sulphated

20.2.2.1.1. Hyaluronic acid

20.2.2.2. Not sulphated

20.2.2.2.1. Chondriotin

20.2.2.2.2. Dermatan

20.2.2.2.3. Heparan

20.2.2.2.4. Keratan