A223 Biochemistry Lesson 1 PDF

Lesson One **[\[SOMETHING'S BREWING\]]** +-------------+-------------+-------------+-------------+-------------+ | **METABOLIS | | | **ENERGY** | | | M** | | | | | +=============+=============+============...

Lesson One **[\[SOMETHING'S BREWING\]]** +-------------+-------------+-------------+-------------+-------------+ | **METABOLIS | | | **ENERGY** | | | M** | | | | | +=============+=============+=============+=============+=============+ | Sum of the | | - Require | | | | chemical | | d | | | | reactions | | to | | | | that is | | maintai | | | | happening | | n | | | | in an | | life | | | | organism. | | process | | | | | | es | | | | 1. [Anabol | | | | | | ism]{.under | | - Synthes | | | | line} | | is | | | | | | of new | | | | Reactio | | molecul | | | | ns | | es | | | | that | | (anabol | | | | build | | ism) | | | | up | | | | | | substan | | - Macromo | | | | ces | | lecules | | | | | | are | | | | 2. [Catabo | | sources | | | | lism]{.unde | | of | | | | rline} | | energy | | | | | | for the | | | | Reactio | | body. | | | | ns | | | | | | that | | - Carbohy | | | | breakdo | | drates | | | | wn | | a major | | | | substan | | source | | | | ces. | | of | | | | | | energy. | | | +-------------+-------------+-------------+-------------+-------------+ | | | | | | +-------------+-------------+-------------+-------------+-------------+ | | | | | | +-------------+-------------+-------------+-------------+-------------+ -------------------------------------------------------- -- **WHY DOES GLUCOSE BREAKDOWN INVOLVES SO MANY STEPS?** -------------------------------------------------------- -- +-----------------------------------+-----------------------------------+ | **Slow Breakdown** | **Fast Breakdown** | +===================================+===================================+ | - Slow breakdown = slow release | - Fast breakdown = fast release | | = more control | = less control | | | | | - Not destructive | - Very destructive | | | | | - Can be used effectively | - Cannot be utilised | | | effectively | | - Stored when not required | | | | - Energy lost as heat/light | | - More efficient | | +-----------------------------------+-----------------------------------+ --------------------------------------------- -- **PATHWAYS OF METABOLISM OF PYRUVATE ACID** --------------------------------------------- -- +-----------------------+-----------------------+-----------------------+ | | **Pyruvate Acid | **Pyruvate Acid | | | Lactic Acid** | Ethanol** | +=======================+=======================+=======================+ | Organism/Tissue in | Humans | Under anaerobic | | which the conversion | | conditions in the | | occurs | | cytosol/cytoplasm. | +-----------------------+-----------------------+-----------------------+ | NADH NAD^+^ | Oxidation reaction is | | | | what cause the | | | | occurrence of change. | | +-----------------------+-----------------------+-----------------------+ | Enzymes involved in | Lactate Dehydrogenase | - Pyruvate | | conversions | | Decarboxylase | | | | | | | | - Alcohol | | | | Dehydrogenase | +-----------------------+-----------------------+-----------------------+ | Purpose of carrying | Produce lactic acid | Produce ethanol when | | out this conversion | when humans undergo | there is insufficient | | | anaerobic | amount of oxygen to | | | (insufficient oxygen) | meet the demands of | | | respiration to meet | the fermentation. | | | demands of the | | | | vigorous muscular | | | | contractions. | | +-----------------------+-----------------------+-----------------------+ ----------------- -- **BEER MAKING** ----------------- -- - Fermented products of grains & cereals. - Yeast (Eukaryote) is involved, a free-living unicellular organism. - Can survive in aerobic & anaerobic conditions --------------------------------------------- -- **INDUSTRIAL APPLICATIONS OF FERMENTATION** --------------------------------------------- -- Diagram Description automatically generated with medium confidence Lesson 1 ---------------- -- **GLYCOLYSIS** ---------------- -- - 10 steps catabolic process to break 1 glucose molecule into 2 pyruvate molecules. - To extract energy for living organisms - Involves breaking down glucose molecules. - Linear Pathway: glucose (substrate) pyruvate (product)  - Energy input stage: 2 ATP required to convert glucose into fructose 1-6 biphosphate. - Energy generation stage: Each 1,3 Diphosphoglceric acid produces 2 ATP & 1 NADH - One glucose yield -- 2 net ATP & 2 NADH. Lesson 1 -------------------- -- **ENERGY STORAGE** -------------------- -- Diagram Description automatically generated - Adenosine Triphosphate (ATP) is the source of energy that all living cells rely on to do everything from building molecules to flexing muscles. - Breaking down ATP = energy released. - Cells constantly replenishing their ATP levels by adding a spare phosphate onto ADP (adenosine diphosphate) - Energy derives from the food we eat (animals) or make (plants) -------------------------------------- -- **WHY DO CELLS DO FERMENTENTATION?** -------------------------------------- --  Cells goes through **fermentation** because it is the only way to generate NAD^+^ to keep glycolysis from happening in anaerobic conditions (insufficient oxygen). Lesson 1 ------------------ -- **FERMENTATION** ------------------ -- Graphical user interface, text, application Description automatically generated - Different cells produce different compounds under anaerobic (insufficient oxygen) conditions 1. **[Muscle cells]** produces lactic acid/lactate resulting in muscle cramps 2. **[Bacterial cells]** produce lactic acid resulting in yoghurt - Initial steps from glucose to pyruvate *(glycolysis)* are the same. - Enzyme responsible for producing lactate is **[Lactate Dehydrogenase]**. Ethanol/Alcohol Fermentation Lactic Acid Fermentation ------------------------------ -------------------------- Plants, Unicells Humans -------------------------- -- **ETHANOL FERMENTATION** -------------------------- --  - Anaerobic condition (insufficient oxygen) - Will take place in both anaerobic respiration & fermentation. - Glycolysis must take place first. (glucose pyruvate) - 1 molecule of Pyruvate = 1 molecule of Ethanol - NAD^+^ = essential by-product of fermentation - Froth (a layer of bubble) = CO2 - Enzymes involved: **[Pyruvate Decarboxylase, Alcohol Dehydrogenase]**. ------------------------------ -- **LACTIC ACID FERMENTATION** ------------------------------ -- **[Lesson 1 Glossary]** +-----------------------+-----------------------+-----------------------+ | 25. | **Metabolism** | Chemical Reactions in | | | | the body's cells | +=======================+=======================+=======================+ | 1. | **Anabolism** | Reactions that build | | | | up substances | +-----------------------+-----------------------+-----------------------+ | 2. | **Catabolism** | Reactions that | | | | breakdown substances | +-----------------------+-----------------------+-----------------------+ | 3. | **Aerobic** | Requires oxygen | +-----------------------+-----------------------+-----------------------+ | 4. | **Anaerobic** | Does not require | | | | oxygen | +-----------------------+-----------------------+-----------------------+ | 5. | **Substrate** | (Enzyme Definition) | | | | | | | | A molecule that an | | | | enzyme reacts with. | +-----------------------+-----------------------+-----------------------+ | 6. | **Enzyme** | Proteins that help | | | | speed up metabolisms | | | | or chemical reactions | | | | in our body. | +-----------------------+-----------------------+-----------------------+ | 7. | **Product** | Anything that is | | | | produced after the | | | | reaction takes place. | +-----------------------+-----------------------+-----------------------+ | 8. | **Glycolysis** | Metabolic pathway | | | | that converts glucose | | | | to pyruvate.\ | | | | it is used to form | | | | adenosine | | | | triphosphate (ATP) & | | | | reduced nicotinamide | | | | adenine dinucleotide | | | | (NADH). | +-----------------------+-----------------------+-----------------------+ | 9. | **Adenosine | Structure -- | | | [Tri]phos | nucleoside | | | phate | triphosphate consists | | | (ATP)** | of a nitrogenous base | | | | (adenine), ribose | | | | sugar & 3 phosphate | | | | group. | | | | | | | | Source of energy for | | | | usage & storage at | | | | cellular level. | +-----------------------+-----------------------+-----------------------+ | 10. | **Adenosine | Important inorganic | | | [Di]phosp | compound in | | | hate | metabolism & | | | (ADP)** | essential the flow of | | | | energy in living | | | | cells. | +-----------------------+-----------------------+-----------------------+ | 11. | **Nicotinamide | Crucial molecules to | | | Adenine Dinucleotide | the body. Coenzyme | | | (NAD/NADH)** | central to | | | | metabolism. | | | | | | | | NAD+ -- Nicotinamide | | | | Adenine Dinucleotide. | | | | | | | | NADH -- Reduced | | | | Nicotinamide Adenine | | | | Dinucleotide | | | | | | | | NAD+ à NADH | | | | (oxidation takes | | | | place) | +-----------------------+-----------------------+-----------------------+ | 12. | **Glyceraldehyde** | Triose monosaccharide | | | | formed as an | | | C~3~H~6~O~3~ | intermediate in | | | | carbohydrate | | | | metabolism by the | | | | breakdown of sugars & | | | | yields a glycerol on | | | | reduction. | +-----------------------+-----------------------+-----------------------+ | 13. | **Dehydration | Creation of larger | | | Synthesis** | molecules from | | | | smaller monomers | | | | where a water | | | | molecule is released. | +-----------------------+-----------------------+-----------------------+ | 14. | **Condensation** | [\[A type of | | | | dehydration | | | | synthesis\]]{.underli | | | | ne} | | | | | | | | 2 smaller molecules | | | | join to form a larger | | | | molecule by removing | | | | a functional group | | | | (i.e., water) | +-----------------------+-----------------------+-----------------------+ | 15. | **Hydrolysis** | [\[Opposite of | | | | Dehydration\]]{.under | | | | line} | | | | | | | | Chemical reaction | | | | where water is used | | | | to breakdown chemical | | | | bonds between | | | | substances. | +-----------------------+-----------------------+-----------------------+ | 16. | **Alcohol | Biotechnological | | | Fermentation** | process accomplished | | | | by yeast, bacteria, | | | | or a few other | | | | microorganisms to | | | | convert sugars into | | | | ethanol & carbon | | | | dioxide. | +-----------------------+-----------------------+-----------------------+ | 17. | **Pyruvate | Enzyme responsible | | | Decarboxylase \[E\]** | for non-oxidative | | | | decarboxylation of | | | | pyruvate to | | | | acetaldehyde & carbon | | | | dioxide. | | | | | | | | (Lyase enzyme) | +-----------------------+-----------------------+-----------------------+ | 18. | **Yeast** | Unicellular | | | | eukaryotic | | | | microorganisms which | | | | is important to | | | | winemaking, baking & | | | | brewing. | +-----------------------+-----------------------+-----------------------+ | 19. | **Acetaldehyde** | (Aldehyde Group) | | | | | | | | Highly reactive & | | | | toxic. It causes | | | | damage at cellular & | | | | genome levels. | | | | Substance is made | | | | from alcohol. | +-----------------------+-----------------------+-----------------------+ | 20. | **Alcohol | Enzyme primarily | | | Dehydrogenase \[E\]** | found in liver & | | | | stomach that | | | | breakdown ethanol to | | | | acetaldehyde which | | | | will be further | | | | broken down into | | | | acetic acid & | | | | converted into carbon | | | | dioxide & water. | +-----------------------+-----------------------+-----------------------+ | 21. | **Ethanol** | Produced by | | | | fermentation. | +-----------------------+-----------------------+-----------------------+ | 22. | **Lactic Acid | Metabolic process | | | Fermentation** | where glucose / other | | | | 6-carbon sugars are | | | | converted into | | | | cellular energy & | | | | metabolite lactate. | | | | (Lactic Acid in | | | | Solution) | +-----------------------+-----------------------+-----------------------+ | 23. | **Lactate | An enzyme found in | | | Dehydrogenase \[E\]** | all body tissue. | | | | | | | | Important role in | | | | cellular respiration | | | | process where glucose | | | | from food is | | | | converted into usable | | | | energy for cells. | +-----------------------+-----------------------+-----------------------+ | 24. | **Lactate / Lactic | Produced in muscle | | | Acid** | cells & red blood | | | | cells.\ | | | | Forms when the body | | | | breakdown | | | | carbohydrate to use | | | | for energy when | | | | oxygen levels are | | | | low. | +-----------------------+-----------------------+-----------------------+ Lesson 2 **[\[AEROBIC RESPIRATION\]]** ------------------------- -- **PYRUVATE PROCESSING** ------------------------- -- - Enters mitochondria from cytoplasm. - NAD^+^ will help oxidise pyruvate into Acetyl CoA by removing a carbon & adding CoA. ----------------- -- **KREBS CYCLE** ----------------- -- - Begins with Acetyl CoA & oxaloacetate (OAA) to produce citric acid - However, 1 glucose molecule = 2 Krebs Cycle to break down completely. +-----------------------------------+-----------------------------------+ | http://www.mikeblaber.org/oldwine | - In the absence of | | /BCH4053/Lecture36/krebs\_02.jpg | dehydrogenase, FAD & NAD^+^ | | | cannot be oxidised into FADH | | | & NADH. | +-----------------------------------+-----------------------------------+ [Is energy produced directly during Krebs Cycle?] Yes, 1 ATP molecule is produced. GTP needs energy to convert to GDP. This energy is obtained when ATP is converted to ADP. -- Coupling Reaction. ---------------------------------------------------------- -- **ELECTRON TRANSPORT CHAIN & OXIDATIVE PHOSPHORYLATION** ---------------------------------------------------------- -- - In electron transport chain, electrons move around. - ETC will regenerate NAD^+^ & FAD for glycolysis, pyruvate processing & Krebs cycle. - Oxidative Phosphorylation oxidises NADH & FADH~2~ & provide energy for ATP synthesis. ------------------ -- **CHEMIOSMOSIS** ------------------ -- - Anything that affects the proton will inhibit the ATP production. - Given that the complex will pump electrons to the intermembrane space, the intermembrane space will have a higher concentration of H+ ions than the mitochondrial matrix. Lesson 2 **[\[AEROBIC RESPIRATION\]]** --------------------------------------------------------------- -- **PROCESS FOR ETC, OXIDATIVE PHOSPHORYLATION & CHEMIOSMOSIS** --------------------------------------------------------------- -- 1. NADH from Krebs Cycle donate electrons to complex I by reducing to NAD^+^ - Complex I get supercharged. *(pump electrons from mitochondria matrix to intermembrane space)* - Proton gradient forms. 2. Once the proton gradient starts forming, the electrons get transported to Coenzyme Q (electron acceptor) 3. At the same time, FADH gets converted to FAD & donates electrons to complex II. *(complex II will not get supercharged.)* 4. The electrons transport to Coenzyme Q and transports electrons to complex III. 5. Complex III gets supercharged & pumps H+ to the intermembrane space. 6. Complex III transports electrons to cytochrome C & then Complex IV. 7. Complex IV gets supercharged, pumping H+ 8. Complex IV pumps electrons to the ultimate electron acceptor -- oxygen (O~2~) *(oxygen is essential for energy production.)* 9. H+ ions will flow from high concentration to low concentration to provide energy to convert ADP to ATP. --------------- -- **ATP COUNT** --------------- -- 1 NADH = 3 ATP 1 FADH = 2 ATP GDP = 1 ATP  Important: Anaerobic respiration -- 2 ATP (from glycolysis) Aerobic respiration -- 38 ATP **[LESSON 2 GLOSSARY]** +-----------------------+-----------------------+-----------------------+ | 5. | **Acetyl CoA** | | +=======================+=======================+=======================+ | 1. | **The Krebs cycle** | | | | | | | | **(Citric acid | | | | cycle)** | | +-----------------------+-----------------------+-----------------------+ | 2. | **Electron | | | | Transport** | | +-----------------------+-----------------------+-----------------------+ | 3. | **Oxidative | | | | Phosphorylation** | | | | | | | | **(Chemiosmosis)** | | +-----------------------+-----------------------+-----------------------+ | 4. | **Flavin Adenine | | | | Dinucleotide** | | | | | | | | **(FAD, FADH~2~)** | | +-----------------------+-----------------------+-----------------------+ Lesson 3 **[\[THERMODYNAMICS\]]** ------------ -- **ENERGY** ------------ -- - Capacity to cause change. - Organisms need a constant source of energy to survive. - Form of energy -- light, mechanical, thermal, electrical etc. -------------------- -- **THERMODYNAMICS** -------------------- -- - Study the flow & transformation of energy in the universe. - **1^st^ Law --** Energy cannot be created or destroyed. It can be converted from one form to another. - 2^nd^ Law -- Energy (disorder) may decrease in organism but the universe' total entropy increases. ∆S~(universe)~ = ∆S~(surroundings)~ + ∆S~(system)~ -------------------- -- **FREE ENERGY ∆G** -------------------- -- - Free energy change of a reaction will tell us whether the **reaction occurs is spontaneous or not**. - ∆G = neg = spontaneous = energy given out exergonic (system able to do work on its own) - ∆G = positive = non-spontaneous = energy taken in endergonic (process have to be forced by external environment -- surroundings to occur) ∆G = ∆H -- T∆S - Free energy diagram shows the change in energy as the reaction progresses. - Shows the difference in energy between reactant (substrate) & product. ---------------- -- **ENDERGONIC** ---------------- -- --------------- -- **EXERGONIC** --------------- -- ----------------------- -- **COUPLED REACTIONS** ----------------------- -- - Endergonic Reaction needed to be coupled to exergonic reaction of a bigger value. - Exergonic reaction & ∆G (Gibbs Free Energy) needs to be positive to proceed. ------------------------------------- -- **WAYS TO REPLENISH ATP MOLECULES** ------------------------------------- -- 1. **[Substrate Level Phosphorylation]** - Phosphate group transferred directly to ADP. (ADP + Pi = ATP) - Form of Biosynthesis -- Substrate-level Phosphorylation - Formation of ATP **[coupled]** to the removal group from another molecule. - Catalysed by various enzymes - Occur in cytoplasm Diagram Description automatically generated 2. **[Oxidative Phosphorylation]** - Process where ATP is formed from Electron Transport Chain from NADH or FADH~2~ - Coupling with Proton Gradient to allow ATP synthesis. - Enzyme involved: ATP Synthase - Occurs in mitochondria **[\ ]** **[LESSON 3 GLOSSARY]** +-----------------------+-----------------------+-----------------------+ | 9. | **1^st^ Law of | | | | Thermodynamics** | | +=======================+=======================+=======================+ | 1. | **2^nd^ Law of | | | | Thermodynamics** | | +-----------------------+-----------------------+-----------------------+ | 2. | **Gibbs Free Energy | | | | (∆G)** | | +-----------------------+-----------------------+-----------------------+ | 3. | **Entropy (∆S)** | | +-----------------------+-----------------------+-----------------------+ | 4. | **Enthalpy (∆H)** | | +-----------------------+-----------------------+-----------------------+ | 5. | **Free Energy | | | | Diagram** | | +-----------------------+-----------------------+-----------------------+ | 6. | **Endergonic | | | | Reaction** | | +-----------------------+-----------------------+-----------------------+ | 7. | **Exergonic | | | | Reaction** | | +-----------------------+-----------------------+-----------------------+ | 8. | **Coupled Reaction** | | +-----------------------+-----------------------+-----------------------+ Lesson 4\ **[\[PROTEINS\]]** +-----------------------+-----------------------+-----------------------+ | **PROTEIN MADE UP | | | | OF?** | | | +=======================+=======================+=======================+ |  | | | | | - Carboxylic Acid | | | | Group | | | | | | | | - Amino Group | | | | | | | | - R Side Chain | | | | (each have a | | | | different | | | | properties) | | +-----------------------+-----------------------+-----------------------+ ----------------- -- **AMINO ACIDS** ----------------- -- A picture containing qr code Description automatically generated *Disulphide bond can only form with those that have sulphur \[S\]* *(cysteine, methlonine)* Lesson 4\ **[\[LEVELS OF PROTEIN FOLDING\]]** ----------------------- -- **PRIMARY STRUCTURE** ----------------------- -- - Linear sequence of amino acids formed (formed from translation at ribosomes) - Peptide/amide bond (covalent) formed. ------------------------- -- **SECONDARY STRUCTURE** ------------------------- -- Interactions between of atoms of one amino acid with atoms of amino acid within the same polypeptide. **[\ ]** - Hydrogen Bond formed between the carbonyl O of one amino acid and amino H of another. (less strong as compared to peptide bond) +-----------------------+-----------------------+-----------------------+ | **α - helix** | Hydrogen bonds formed | | | | from up to down. | | +=======================+=======================+=======================+ | | **[Bonds | 3. Between N -- H & | | | formed:]* | R group | | | * | | | | | 4. Between R groups | | | 1. Between C = O & N | | | | -- H group | | | | | | | | 2. Between C = O & R | | | | group (amino | | | | acid) | | +-----------------------+-----------------------+-----------------------+ | **β -- pleated | Hydrogen bonds formed | | | sheet** | from left to right | | | | | | | | **[Bond | | | | formed:]* | | | | * | | | | between C = O & N -- | | | | H group | | +-----------------------+-----------------------+-----------------------+ ------------------------ -------------- **TERTIARY STRUCTURE** (one strand) ------------------------ -------------- Interaction between various α-helices & β -- pleated sheets (from secondary structure) to form a 3-dimension structure. -- ------------------------  -- ------------------------ **[Bonds formed:]** 1. 2. Disulfide Bridge Bond 3. Ionic Interactions 4. Hydrophobic Interactions 5. Hydrophilic Interactions -------------------------- -- **QUATERNARY STRUCTURE** -------------------------- -- Complex of more than 1 polypeptide chain. - Hydrogen bonds & Disulphide bonds formed between polypeptide chain. Lesson 4 **[\[BONDS IN PROTEINS\]]** --------------------------------------------- -- **TYPE OF FORCES HOLDING PROTEIN TOGETHER** --------------------------------------------- -- 1. Hydrogen Bonds 2. Covalent Bonds 3. Ionic Bonds 4. Hydrophobic & hydrophilic interaction, electrostatic ------------------------ -- **STRENGTHS OF BONDS** ------------------------ -- **Bond Type** **Energy (kJ/mol)** ------------------ --------------------- Covalent 350 Disulphide (S-S) 60 -- 80 Electrostatic 15 van der Waal's 10 Hydrogen 21 **FORMATION OF INTERMOLECULAR BOND** -------------------------------------- --  - Hydrophobic side chain = repel water - Hydrophilic side chain = attract water - Hydrogen bonds are formed -- stabilising effect on the structure. - Presence of water will force the hydrophobic residues to cluster inside the protein which makes them interact. ------------------ -- **DENATURATION** ------------------ -- Process where protein loses its quaternary structure, tertiary structure & primary structure (unfolded & inactivated), resulting in a loss of functions and unable to work properly. ------------------------------- -- **FACTORS AFFECTING FOLDING** ------------------------------- -- - High temperature = reduces strength of hydrogen bonds *(non-covalent bonds break easily)* - Extreme pH levels = alters electrostatic interactions between charged amino acids -- basic & acidic ------------------------------------- -- **TYPE OF TERTIARY LEVEL PROTEINS** ------------------------------------- -- **FIBROUS PROTEINS** **GLOBULAR PROTEINS** --------------------- ------------------------------------------------------------------------------ ---------------------------------------------------------------  A picture containing text Description automatically generated Shape Long & Narrow Spherical / Round Function Structural roles Functional Roles Amino Acid Sequence Repetitive amino acid sequence Irregular amino acid sequence Durability Less sensitive to changes in pH, temperature etc. More sensitive to changes in pH, temperature etc. Solubility Insoluble in water Soluble in water Examples Collagen, myosin, fibrin, actin, keratin & elastin Enzymes, Haemoglobin, Insulin, Immunoglobulin (antibodies) ----------------------------- -- **HOW IS COLLAGEN FORMED?** ----------------------------- -- - Collagen is very tightly folded protein. - 3 chains coil together to form tropocollagen. - Tropocollagen will form interchain bonds to assemble into collagen fibres. - Fibres are very tough & insoluble in water. - Make up an estimation of 30% of bone tissue. ---------------------------- -- **HOW IS GELATIN FORMED?** ---------------------------- --  ------------------------- -- **COLLAGEN VS GELATIN** ------------------------- -- *\*amino acid sequence is identical* +-----------------------+-----------------------+-----------------------+ | | **COLLAGEN** | **GELATIN** | +=======================+=======================+=======================+ | Protein Structure | - High degree of | - Protein unfolded. | | | protein folding | | | | | - All | | | - Intermolecular & | intermolecular | | | Inter-polypeptide | bonds are broken. | | | chain bonds | | | | | - No secondary -- | | | - Stable quaternary | quaternary | | | structures | structure | +-----------------------+-----------------------+-----------------------+ | Physical Properties | Tough, fibre-like & | Soft, jelly-like & | | | insoluble in water | soluble water | +-----------------------+-----------------------+-----------------------+ | Function | Structural component | Provides textural | | | of skin, bones & | effects. | | | connective tissues | | | | | (i.e., thickening & | | | | gelling) | +-----------------------+-----------------------+-----------------------+ **[LESSON 4 GLOSSARY]** +-----------------------+-----------------------+-----------------------+ | 19. | **Amino Acid** | Proteins are made up | | | | of monomers. | +=======================+=======================+=======================+ | 1. | **Amino Group & | Parts of an amino | | | Carboxylic Group** | acid structure. | +-----------------------+-----------------------+-----------------------+ | 2. | **R-side Chain** | Components that | | | | determine property & | | | | how the amino acid | | | | looks like. | +-----------------------+-----------------------+-----------------------+ | 3. | **Non-polar Amino | Little / no polarity | | | Acids (hydrophobic)** | in their side chain. | | | | | | | | Unable to interact | | | | with highly polar | | | | water molecules -- | | | | water fearing. | +-----------------------+-----------------------+-----------------------+ | 4. | **Polar Amino Acids | More soluble in water | | | (hydrophilic)** | & able to form | | | | hydrogen bonds with | | | | water because of | | | | functional group. | +-----------------------+-----------------------+-----------------------+ | 5. | **Acidic Amino | Have a pH 7.0. -- | | | Acids** | negative charged | | | | | | | | The amino acids will | | | | be negatively charged | | | | & have a second | | | | carboxyl group. | +-----------------------+-----------------------+-----------------------+ | 6. | **Basic Amino Acids** | Significant positive | | | | charge at pH 7.0 -- | | | | positively charged. | +-----------------------+-----------------------+-----------------------+ | 7. | **Peptide Bond** | Bonds formed when | | | | connecting 2 amino | | | | acids. | | | | | | | | NH~2~ of amino acid | | | | -- COOH group of | | | | amino acid through | | | | dehydration. | | | | | | | | (covalent bond) | +-----------------------+-----------------------+-----------------------+ | 8. | **Hydrogen Bond** | Formed between | | | | peptide groups -- | | | | between side chain & | | | | peptide group between | | | | 2 side chain. | | | | (covalent bond) | +-----------------------+-----------------------+-----------------------+ | 9. | **Ionic Bond** | Electrostatic | | | | attraction between | | | | opposite charged | | | | ions. | +-----------------------+-----------------------+-----------------------+ | 10. | **Hydrophobic | Large contribution to | | | Interactions** | the stability of | | | | protein structures. | +-----------------------+-----------------------+-----------------------+ | 11. | **Disulphide Bond** | Stabilises tertiary & | | | | quaternary structure | | | | of proteins. | | | | (covalent bond) | +-----------------------+-----------------------+-----------------------+ | 12. | **Primary Structure** | Sequence of amino | | | | acids -- only for | | | | peptide bonds. | +-----------------------+-----------------------+-----------------------+ | 13. | **Secondary | Local folded | | | Structure** | structures formed | | | | within a polypeptide | | | | due to interactions | | | | between atoms of | | | | backbone. | | | | | | | | Common: a-helices & | | | | B-pleated sheet. | | | | | | | | (Hydrogen bonds | | | | between NH~2~ & -COOH | | | | group) | +-----------------------+-----------------------+-----------------------+ | 14. | **Tertiary | Interactions between | | | Structure** | secondary structures | | | | to form 3D structure. | | | | -- one strand. | | | | | | | | Hydrogen bonds | | | | between side chain, | | | | hydrophobic | | | | interactions, | | | | disulphide bridge & | | | | ionic bonds. | +-----------------------+-----------------------+-----------------------+ | 15. | **Quaternary | Complex of more than | | | Structure** | 1 polypeptide chain. | | | | | | | | (Hydrogen & | | | | Disulphide bonds | | | | between polypeptide | | | | chain) | +-----------------------+-----------------------+-----------------------+ | 16. | **Denaturation** | Unfolding of proteins | | | | & lose their | | | | functions. | +-----------------------+-----------------------+-----------------------+ | 17. | **Collagen** | Tightly folded | | | | proteins -- 3 chains | | | (Fibrous proteins) | coiled together to | | | | form interchain bonds | | | | to assemble into | | | | collage fibres. | +-----------------------+-----------------------+-----------------------+ | 18. | **Gelatin** | Proteins unfolded -- | | | | no secondary to | | | | quaternary structure | | | | do not exist. | +-----------------------+-----------------------+-----------------------+ Lesson 5 **[\[CHARACTERISTICS OF ENZYMES\]]** ----------------------- -- **WHAT ARE ENZYMES?** ----------------------- -- - Enzymes are proteins. - Biological catalysts that lower activation energy \[Ea\] which can speed up biochemical reaction. - It is reusable. ----------------- -- **ACTIVE SITE** ----------------- -- - Enzyme must bind to substrate here. - Formed from protein folding. - Complementary in shape to substrate --------------------- -- **ALLOSTERIC SITE** --------------------- -- Allow molecules to either activate or inhibit enzyme activities. (More in L06) --------------------------- -- **LOCK & KEY HYPOTHESIS** --------------------------- -- Substrate fits precisely into active site of enzyme (Made for the substrate to fit) ---------------------------------- -- **INDUCED-FIT MODEL HYPOTHESIS** ---------------------------------- -- Substrate & Active Site will both alter the shape accordingly during process of binding. -------------------------------- -- **CLASSIFICATIONS OF ENZYMES** -------------------------------- -- - Names are based on what it reacts with or how does it react. - Common types of enzymes: +-----------------+-----------------+-----------------+-----------------+ | **Group Name** | **Type of | | | | | Reaction | | | | | Catalysed** | | | +=================+=================+=================+=================+ | Oxidase / | Redox Reactions | | | | Dehydrogenase | | | | | or Reductase | *(oxidation -- | | | | | reduction)* | | | +-----------------+-----------------+-----------------+-----------------+ | Transferase | Transfer of | | | | | functional | | | | | groups | | | +-----------------+-----------------+-----------------+-----------------+ | Hydrolase | Hydrolysis | | | | | reactions | | | | | | | | | | *(addition of | | | | | water | | | | | molecule)* | | | +-----------------+-----------------+-----------------+-----------------+ | Lyase | Addition to | | Breaking of | | | double bonds | | bonds to form | | | | | double bond | +-----------------+-----------------+-----------------+-----------------+ | Isomerase | Isomerization | | | | | reactions | | | +-----------------+-----------------+-----------------+-----------------+ | Ligase | Uses ATP | | | | | hydrolysis to | | | | | perform its | | | | | function | | | +-----------------+-----------------+-----------------+-----------------+ --------------- -- -- **CATALYSTS** --------------- -- -- Diagram Description automatically generated Able to reduce the activation energy \[Ea\] of the reaction drastically. **[\[FACTORS AFFECTING ENZYME ACTIVITY\]]** ---------------------- -------------------------------------- **HIGH TEMPERATURE** (exceed optimum temperature of 37˚C) ---------------------- -------------------------------------- *Effective binding & catalysis cannot take place.* - Enzymes denature when hydrogen bonds break. - Active Sites destroyed as protein folding is destroyed too. - Active Site destroyed Substrate cannot bind. --------------------- -- **LOW TEMPERATURE** --------------------- -- *Effective binding & catalysis is lower since temperature have decrease.* - Temperature too low = Kinetic Energy decreases - Decrease in Kinetic Energy Less chances for effective collision between substrate & enzyme. ---------------------------------------- -- **pH LEVEL IS NOT NEUTRALISED (pH 7)** ---------------------------------------- -- *Effective binding & catalysis cannot take place.* - pH deviates, electrostatic interactions between acidic & basic amino acids are affected. - Result in Protein Denaturation Active Site destroyed Binding unable to occur. -------------------------- -- **ENZYME CONCENTRATION** -------------------------- -- - Increase Enzyme Concentration = Increase Rate of Reaction - Number of active sites available for reaction particles to bind to (increases per unit time) - Until substrate becomes the limiting factor - Therefore, more active sites than substrate molecules. ----------------------------- -- **SUBSTRATE CONCENTRATION** ----------------------------- -- - Increases Substrate = Increase Rate of Reaction - Probability of reaction particles colliding increases - Reaction particles with energy more than activation energy colliding increases **[until saturation point reached]**. **[\ ]** **[LESSON 5 GLOSSARY]** +-----------------------+-----------------------+-----------------------+ | 14. | **Catalyst** | Reduces activation | | | | energy \[Ea\] of a | | | | reaction. | | | | | | | | Helps to speed up the | | | | rate of reaction | | | | without changing | | | | overall free energy. | +=======================+=======================+=======================+ | 1. | **Oxidase / | Also known as | | | Dehydrogenase or | oxidation -- | | | Reductase** | reduction reactions. | | | | | | | | Hydrogen transfer | | | | (Dehydrogenase) to | | | | acceptor compound | | | | (Reductase) | +-----------------------+-----------------------+-----------------------+ | 2. | **Transferase** | Transfer of | | | | functional group from | | | | a donor substrate | | | | \[S\] to an acceptor | | | | compound. | +-----------------------+-----------------------+-----------------------+ | 3. | **Hydrolase** | Involves hydrolysis | | | | -- addition of water. | +-----------------------+-----------------------+-----------------------+ | 4. | **Lyase** | Functional group | | | | added to double | | | | bonds. | | | | | | | | Double bonds formed | | | | due to removal of | | | | functional groups. | | | | | | | | (either way are | | | | doable) | +-----------------------+-----------------------+-----------------------+ | 5. | **Isomerase** | Interconversion of | | | | isomers. | | | | | | | | (Sharing the same | | | | atomic composition | | | | but different | | | | arrangements of | | | | chemical groups) | +-----------------------+-----------------------+-----------------------+ | 6. | **Ligase** | Formation of bonds | | | | with ATP cleavage -- | | | | ATP Hydrolysis occur. | | | | | | | | *Separation of | | | | phosphate group from | | | | ATP -- ATP to ADP.* | +-----------------------+-----------------------+-----------------------+ | 7. | **Active Site** | Enzyme binds to | | | | substrate here. | | | | | | | | Formed because of | | | | protein folding -- | | | | secondary, tertiary & | | | | quaternary. | +-----------------------+-----------------------+-----------------------+ | 8. | **Lock & Key | Substrate \[S\] fits | | | Hypothesis** | precisely into the | | | | active site of the | | | | enzyme. | +-----------------------+-----------------------+-----------------------+ | 9. | **Induced Fit | Substrate of active | | | Hypothesis** | site will change | | | | shape slightly during | | | | process of binding. | +-----------------------+-----------------------+-----------------------+ | 10. | **Progress Curve** |  | | | | | | | | Progress of reaction | | | | measured over time | | | | (t). | | | | | | | | Substrate finishing = | | | | rate of production | | | | formation decreases. | +-----------------------+-----------------------+-----------------------+ | 11. | **The | Chart, line chart | | | Michaelis-Menten | Description | | | Curve** | automatically | | | | generated | | | **(MM Curve)** | | | | | Progress curve | | | | measured to form 1 MM | | | | curve. | | | | | | | | Initial Velocities | | | | plotted against | | | | substrate | | | | concentration. | | | | | | | | Shows relationship | | | | between velocity & | | | | substrate | | | | concentration. | +-----------------------+-----------------------+-----------------------+ | 12. | **Maximum Velocity | Enzymes are working | | | (V~max~)** | at full capacity. | | | | (Rate of reaction | | | | cannot increase) | +-----------------------+-----------------------+-----------------------+ | 13. | **Substrate | Strength of affinity | | | Concentration | (attraction between 2 | | | (K~m~)** | substrate) between | | | | enzymes & substrate. | +-----------------------+-----------------------+-----------------------+ **[\ LESSON 6 GLOSSARY]** +-----------------------+-----------------------+-----------------------+ | 11. | **Enzyme Inhibitor** | Molecules that | | | | interact in some ways | | | | with the enzyme which | | | | prevents it from | | | | working in a normal | | | | manner. | +=======================+=======================+=======================+ | 1. | **Non-Specific | Denaturation of | | | Inhibitor** | enzymes occurs. | | | | | | | | (E.g., Temperature, | | | | pH levels) | +-----------------------+-----------------------+-----------------------+ | 2. | **Denaturation** | Unfolding proteins. | | | | Losing the secondary, | | | | tertiary & quaternary | | | | structure. | +-----------------------+-----------------------+-----------------------+ | 3. | **Reversible Enzyme | Bind loosely to | | | Inhibitor** | active site but can | | | | dissociate from | | | *(specific)* | enzyme. | +-----------------------+-----------------------+-----------------------+ | 4. | **Irreversible Enzyme | Bind tightly to | | | Inhibitor** | enzyme's active site | | | | preventing substrate | | | *(specific)* | from binding to | | | | enzyme. | +-----------------------+-----------------------+-----------------------+ | 5. | **Competitive | Inhibitors bind to | | | Inhibition** | enzyme's active site | | | | to prevent substrate | | | *(reversible)* | from binding. | +-----------------------+-----------------------+-----------------------+ | 6. | **Non-Competitive | Inhibitors bind to | | | Inhibition** | allosteric site which | | | | interferes with | | | *(reversible)* | enzymatic activities. | +-----------------------+-----------------------+-----------------------+ | 7. | **Covalent Bond** | Strongest bonds. | | | | | | | | (Occur in | | | | irreversible | | | | inhibitors) | +-----------------------+-----------------------+-----------------------+ | 8. | **Non-Covalent Bond** | | +-----------------------+-----------------------+-----------------------+ | 9. | **Allosteric Site** | Alternative binding | | | | site for inhibitor. | | | | | | | | (non-competitive) | +-----------------------+-----------------------+-----------------------+ | 10. | **Feedback | Product of a reaction | | | Inhibition** | interferes with the | | | | enzyme that helped | | | | produced it. | +-----------------------+-----------------------+-----------------------+ Lesson 7 **[\[ENZYMATIC ACTIVITY IN LAB\]]** ----------------------- -- **SPECTROPHOTOMETER** ----------------------- --  - More absorbance = more yellow = more product formed - Produce light at a selected wavelength (**λ**). - Light is passed through the samples. - Sample will absorb certain amount of light. - Remaining light will be detected by a photometer. - Photometer -- send voltage signals to a display device. **[HOW TO USE A SPECTROPHOTOMETER?]** 1. Select \ 2. Select \ 3. Press \ (SmplCmpt) key 4. Use (GO TO WL) key to set the wavelength. 5. Press 1 to select \ 6. Select \, Press ENTER 7. Put in the Blank (control) and Samples in the sequence of 1-6 8. Press \ key at (Cell Position 1) -- will hear a beep sound. 9. Press \(move cell) key to desired cell position. 10. Absorbance value will be shown at the top right-hand corner of the screen. 11. Press \ (Cell 1) after finish reading all samples. ---------------- -- **ABSORBANCE** ---------------- -- Logarithmic measurement of amount of light absorbed (at a particular wavelength) as the light passes through the sample. ---------------- -- **BEER'S LAW** ---------------- -- Absorbance is proportional to the cell path length & concentration of light-absorbing analyte. More light absorbed = more analyte in sample -------------------- -- **STANDARD CURVE** -------------------- -- Chart, line chart Description automatically generated - Use to find unknown concentration of analyte - Using standards with known concentration of the analyte: *Start by diluting a known concentration of the analyte to the range of concentration* - Measure absorbance of each concentration & the unknown - Plot absorbance (y-axis), concentration (x-axis) - Use the straight line to obtain concentration of unknown sample.  **[LESSON 7 GLOSSARY]** +-----------------------+-----------------------+-----------------------+ | 7. | **Cellulase** | Breaks down cellulose | | | | molecules into | | | | monosaccharides. | +=======================+=======================+=======================+ | 1. | **Endocellulase** | Hydrolyses glycoside | | | | links within | | | | cellulose chains. | +-----------------------+-----------------------+-----------------------+ | 2. | **Exocellulase** | Releasing cellobiases | | | | from non-reducing | | | | ends of cellulose. | +-----------------------+-----------------------+-----------------------+ | 3. | **Cellobiases** | Involved in last stop | | | | of breaking down | | | | cellulose. | +-----------------------+-----------------------+-----------------------+ | 4. | **Spectrophotometer** | Produces light of a | | | | selected wavelength. | | | | | | | | Remaining light | | | | detected by a | | | | photometer, sending a | | | | voltage signal to | | | | display signal. | +-----------------------+-----------------------+-----------------------+ | 5. | **Absorbance** | Logarithmic | | | | measurement of light | | | | absorbed as the light | | | | passes through a | | | | sample. | +-----------------------+-----------------------+-----------------------+ | 6. | **Beer's Law** | Absorbance is | | | | proportional to cell | | | | path length & | | | | concentration of | | | | light absorbing | | | | analyte. | +-----------------------+-----------------------+-----------------------+ \[Mostly in Fungi\] experiments about Fungi. Lesson 8 **[\[GLYCOGEN\]]** ---------------------- -- **WHAT IS GLUCOSE?** ---------------------- -- - Carbohydrate monomer - [2 Types of Monomers:] Diagram, schematic Description automatically generated -------------------------------------------- -- **WHY IS GLUCOSE NOT STORED IN THE BODY?** -------------------------------------------- -- - Soluble in water - Able to diffuse out of the cell via its concentration gradient. - Makes it impossible to keep glucose in the cells. ----------------------- -- **WHAT IS GLYCOGEN?** ----------------------- -- - Highly branched carbohydrate polymer. - A large molecule -- therefore, less soluble in water compared to glucose & unable to diffuse easily.  **α -- 1,4 glycosidic bonds:** joins linear α -- glucose molecules **α -- 1,6 glycosidic bonds:** joins branched α -- glucose molecules together. ---------------------------------------------- -- **WHY IS BRANCHING ESSENTIAL FOR GLYCOGEN?** ---------------------------------------------- -- - More branches = rapid release of glucose from glycogen increases. - Branching creates more non-reducing ends for enzymatic attacks for rapid release of glucose. **[Reducing vs Non-Reducing Ends]** 1. Reducing ends à free carbon number 1 with no branching at all 2. Non-reducing ends (used as active sites for enzymes) à Do not have a free carbon-1 with branching. *Non reducing ends à can be used for rapid release of glucose.* ------------------------------------------- -- **WHY ATP CANNOT BE STORED IN THE BODY?** ------------------------------------------- -- - Unstable molecule -- dissolve in water quickly. - ATP breaks down to form ADP + Pi (Inorganic Phosphate) = release energy - ATP will need to be constantly regenerated through cellular respiration if we use this as a storage of energy. - ATP will not be used as a form of storage of energy & it is not ideal. ATP à ADP + Pi (hydrolysation -- addition of water molecule) ----------------------------- -- **HIGH CARBOHYDRATE DIETS** ----------------------------- -- - High carbohydrate diet = High amount of glucose during digestion. - Starch can be found in this food which will be broken down into glucose during digestion. - In small intestines, glucose molecules are transported into body for energy production (ATP) - ATP production maintains or decrease when there is low requirement for ATP. - Excess glucose is converted to glycogen for storage -- glycogenesis. - Carbohydrate loading -- increases endurance time before exhaustion level is reached. (athletes) ------------------------------ ---------------- **ENERGY RELEASE IN MUSCLE** (for athletes) ------------------------------ ---------------- - Working muscles cells require a fast & constant supply of glucose for ATP production - Glycogen stored in muscle -- provides glucose *(in the form of G6P)* for these muscle cells - Rapid release of glucose from glycogen is possible by the many branched ends of glycogen. - Branching would create a lot of ends for enzymatic attack for rapid release of glucose. - Carbohydrate Loading à increase carbohydrate intake à glycogen storage increase ------------------ --------------------------- **GLYCOGENESIS** \[Formation of Glycogen\] ------------------ --------------------------- Rate Limiting Enzyme: **[Glycogen Synthase]** +-----------------------------------+-----------------------------------+ | ![Application Description | **[Steps:]** | | automatically generated with | | | medium | 1. Glucose will be converted | | confidence](media/image30.png) | into Glucose-6-phosphate by | | | attaching a phosphate group | | | on the 6^th^ carbon of the | | | glucose molecule using | | | Hexokinase. | | | | | | (Requires ATP ADP + Pi to | | | allow conversion) | | | | | | 2. Phosphoglucomutase will shift | | | the phosphate group on the | | | 6^th^ carbon to the 1^st^ | | | forming Glucose-1-Phosphate. | | | | | | 3. UDP-Glucose Pyrophosphorylase | | | removes 2 phosphate group | | | from UTP to form UDP to | | | release energy for reaction | | | to be completed. (UDP-Glucose | | | formed) | | | | | | 4. UDP Glucose will be catalysed | | | into glycogen using glycogen | | | synthase which will remove | | | UDP from the glucose. | | | | | | 5. Glucose will be formed & it | | | will be added on to the | | | polymer. | +-----------------------------------+-----------------------------------+ **[Chemical Structures:]** 1. [Uridine Triphosphate] 2. [UDP -- Glucose]  UDP + Pi (phosphate group) UTP. 3. -------------------- ---------------------------------------------------- **GLYCOGENOLYSIS** \[Breakdown of Glycogen\] -- create a few pathways -------------------- ---------------------------------------------------- Text Description automatically generated - Anaerobically generated. - 3 ATP is formed from per glucose -- from glycogen. **[Steps:]** 1. Glycogen phosphorylase will cleave a 1,4 glycosidic bond between the glucose residues. It will catalyse the transfer for 1 phosphate group to the free glucose. *Process will release a glucose-1-phsophate at a time until 4 glucose is left.* 2. Glucose-1-phosphate will be converted to glucose-6-phosphate by phosphoglucomutase. 3. Glucose-6-phosphate will go in different directions... +-----------------------------------+-----------------------------------+ | **Liver** | - Glucose-6-Phosphatase can be | | | found in the liver only. | | | | | | - Releases free glucose into | | | bloodstream for other organs | | | & tissues to use. | +===================================+===================================+ | **Muscles / Brain** | - Do not have | | | Glucose-6-Phosphatase. | | | | | | - Sent to glycolysis pathway to | | | make energy for running if it | | | is required to be broken | | | down. | +-----------------------------------+-----------------------------------+ **[Take Note:]** - Glycogen Glucose-6-Phosphate instead of glucose as it does not diffuse into the cell membrane & undergo glycolysis (Prevent waste of ATP) - Muscle cell does not have Glucose-6-Phosphatase = Glucose-6-Phosphate undergo glycolysis. **[LESSON 8 GLOSSARY]** +-----------------------+-----------------------+-----------------------+ | 23. | **Glucose** | Type of | | | | monosaccharides of | | | | carbohydrates & it is | | | | a monomer. | | | | | | | | Types of glucose: | | | | α-glucose & β-glucose | +=======================+=======================+=======================+ | 1. | **α-glucose** | It is less stable | | | | than **β-glucose** | | | *(OH group below)* | due to its | | | | orientation of | | | | hydroxyl (OH) group. | | | | Higher in energy, | | | | lower melting point | | | | than **β-glucose -- | | | | 146ºC**, more | | | | reactive to enzymes. | +-----------------------+-----------------------+-----------------------+ | 2. | **β-glucose** | Lesser in energy than | | | | **α-glucose**, | | | *(OH group above)* | melting point of | | | | 150ºC & less reactive | | | | to enzymes because | | | | they are harder to be | | | | break down. | +-----------------------+-----------------------+-----------------------+ | 3. | **Glycogen** | Carbohydrate polymer | | | | & used for storage of | | | | glucose to be broken | | | | down into ATP in the | | | | liver. Made up of | | | | glucose that is | | | | linked by glycosidic | | | | bonds. | +-----------------------+-----------------------+-----------------------+ | 4. | **[α-1,4] | Covalent bond between | | | -glycosidic | a hydroxyl (OH) group | | | bond** | on carbon 1 of a | | | | glucose molecule to | | | | another hydroxyl | | | | group of another | | | | glucose molecule. | +-----------------------+-----------------------+-----------------------+ | 5. | **[α-1,6] | Found in every 10 | | | -glycosidic | (estimated) glucose | | | bond** | molecules to create | | | | branches to allow | | | | more access to | | | | glycogen. | +-----------------------+-----------------------+-----------------------+ | 6. | **Glyco[genesis]{.und | Synthesis of glucose | | | erline}** | to form glycogen | | | | | | | | Excess glucose will | | | | undergo glycogenesis | | | | to form glycogen & | | | | store it in the | | | | liver. | +-----------------------+-----------------------+-----------------------+ | 7. | **Glyco[genolysis]{.u | Breakdown of glycogen | | | nderline}** | into glucose. | | | | | | | | The glycogen in the | | | | liver will be broken | | | | down when there is | | | | insufficient | | | | energy/food | | | | consumption to allow | | | | formation of glucose | | | | to make ATP | | | | immediately. | +-----------------------+-----------------------+-----------------------+ | 8. | **Starch** | Found in high | | | | carbohydrate level | | | | food that has a | | | | similar structure to | | | | glycogen. | +-----------------------+-----------------------+-----------------------+ | 9. | **Hexokinase \[E\]** | To start glycolysis | | | | -- catalyses the | | | | phosphorylation of | | | | glucose by ATP to | | | | convert it into | | | | glucose-6-phosphate. | | | | | | | | (Rate limiting enzyme | | | | in glycolysis) | +-----------------------+-----------------------+-----------------------+ | 10. | **Glucose-1-phosphate | A glucose molecule | | | ** | with phosphate on | | | | carbon 1. It is the | | | | first step before | | | | glucose-6-phosphate | | | | is made. | +-----------------------+-----------------------+-----------------------+ | 11. | **Glucose-6-Phosphate | Found in the muscles | | | (G6P)** | -- provides glucose | | | | when starving. | +-----------------------+-----------------------+-----------------------+ | 12. | **Phosphoglucomutase | Key enzyme in | | | \[E\]** | glycolysis & | | | | gluconeogenesis. | | | | | | | | It catalyse the | | | | reaction of | | | | Glucose-6-phosphate | | | | into | | | | Glucose-1-phosphate | | | | by moving phosphate | | | | group on to the | | | | glucose monomer | | | | carbon location (1 or | | | | 6). | +-----------------------+-----------------------+-----------------------+ | 13. | **UDP-Glucose | UDP -- Uridine | | | Pyrophosphorylase** | diphosphate | | | | | | | | [2 Conversions take | | | | place:] | | | | | | | | 1. UTP PPi (Forms | | | | UDP) | | | | | | | | 2. Catalyse | | | | glucose-1-phospha | | | | te | | | | which allows | | | | UDP-glucose to be | | | | formed next which | | | | will undergo a | | | | reaction to | | | | create glucose. | +-----------------------+-----------------------+-----------------------+ | 14. | **Glycogen Synthase | Essential for | | | \[E\]** | glycogenesis -- | | | | glucose into | | | | glycogen. | | | | | | | | Upon UDP-glucose | | | | being catalysed, UDP | | | | will be removed which | | | | will form glucose. | | | | Glucose monomer will | | | | join the glycogen | | | | polymer. | +-----------------------+-----------------------+-----------------------+ | 15. | **Glucose-6-Phosphata | A type of enzyme | | | se | found in the liver. | | | (G6Pase) \[E\]** | It catalyse the | | | | conversion of | | | | glucose-6-phosphate | | | | to glucose by | | | | removing the | | | | phosphate group. | +-----------------------+-----------------------+-----------------------+ | 16. | **Glycogen | It is the main enzyme | | | Phosphorylase \[E\]** | to allow | | | | glycogenolysis to | | | | take place. The main | | | | role of this is to | | | | provide sufficient | | | | energy for muscle | | | | contraction. | | | | | | | | Act as a catalyse to | | | | form | | | | glucose-6-phosphate. | | | | It catalyses the | | | | release of glucose | | | | monomers from the | | | | glycogen polymer | | | | stored in the liver. | +-----------------------+-----------------------+-----------------------+ | 17. | **Ketone Bodies** | Produced by the liver | | | | to serve as an energy | | | | source when glucose | | | | is unavailable. Main | | | | ketone bodies -- | | | | acetoacetate (AcAc) & | | | | 3-beta-hydroxybutyrat | | | | e | | | | (3HB). | +-----------------------+-----------------------+-----------------------+ | 18. | **Ketogenesis** | Metabolic pathway | | | | that produces ketone | | | | bodies which provide | | | | an alternative form | | | | of energy in the | | | | liver. Can make up to | | | | 22 ATP in each | | | | circumstance -- | | | | regulated by insulin. | | | | | | | | (Initiated only when | | | | the body does not | | | | have sufficient | | | | glucose) | +-----------------------+-----------------------+-----------------------+ | 19. | **Pentose Phosphate | \[Branch out from | | | Pathway (PPP)** | glucose-6-phosphate\] | | | | | | | | Produces NADPH & | | | | ribose-5-phosphate. | | | | | | | | It is a major | | | | regulator for | | | | cellular redox | | | | homeostasis & | | | | biosynthesis. | +-----------------------+-----------------------+-----------------------+ | 20. | **Reduced | It provides reducing | | | Nicotinamide Adenine | power that drives | | | Dinucleotide | nu