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EUKTARYOTE animal cell - Lysosome (digest) PROKARYOTE...

EUKTARYOTE animal cell - Lysosome (digest) PROKARYOTE macrotubules , Skytoskeleton membrane size ~ Membrane ~ Cytoplasm presence of V cytoplasm plant cell-cell wall (more rigia) DNA NOT in nucleus nucleus in DNA in nucleus vacuole (pressure) membrane bound v Ribosomes / Ribosomes 0 2-2 MCM 10-100 mcm MODULE 2: BIOCHEMISTRY. nucleoid region ↓ the nucleus X Plasmid DNA multiple linear complex simple Mitosis/Meiosis (PMAT) Prepared by: Louise Theunis, RPh Binary fission (Bind Divide & - science concerned with the chemical constituents of living weak oxidizing agent : Aldehyde > dicarboxylic > - carboxylic aldaric acid = aldonic Acid strong : Both ends = - cells & with the reactions & process they undergo. Reactions of Carbohydrates: strong protection + : In Oxidized = uronic - basic unit of life: cell 1. Oxidation: aldonic acid, aldaric acid, uronic acid - Biomolecules 2. Reduction of Monosaccharides (to alcohol/polyol) 1. Carbohydrates 3. Glycosidic bond formation via condensation (loss molecules of water hydrolyse (add) 2. Proteins 4. Dehydration (action of Acid) 3. Lipids Molisch Test or Alpha- general test for Carbohydrates Blue black-starch 4. Nucleic Acids Naphthol Reaction (+) purple colored ring Iodine No-simpler test : 1KI carbs Mono , glycosidic Bond Bial’s Test (orcinol) for pentoses (+) Green/blue if not = - nexose CARBOHYDRATES CHO Tollen’s Test (+) violet-red 36 - hydrates of carbon; polyhydroxyaldehydes/ketones; CHO * Seliwanoff’s Test for Ketones; differentiates aldose carbon chemy - Uses: energy, structural, pharmaceutic, pharmacologic Hydrogen Oxygen or“Resorcinol Test” (pink) & ketose (red) sugars Tauber’s Test or for ketoses One , single cannot be broken down Aminoguanidine Rxn (+) Reddish purple , gly-tr-ga MONOSACCHARIDES - glucose , fructose galactose , (single sugar) Mal- Syc-19 DISACCHARIDES - 2 sugar molecules linked 5. Reactions w/ Oxidizing Agents: Reducing Sugars OLIGOSACCHARIDES Benedicts Test Trace sugar =green NO RX - reducing Non star-gly-cell POLYSACCHARIDES -many sugar molecule linked Red-reducing Moderate amt = yellow/orange Ball & stick Model Wedge & Dash Projection - Wedge (towards) , Dash (away Big amt = red orange or red Fisher Projection Barfoed’s Test Distinguishes mono- from 2, alcose Red 2-3 (Mono) - 12-letose disaccharides Red After 10 (Di HNOz Nitric Acid Internal Cs-chiral penultimate Aldose C2 (3(4-righ side-down Mucic Acid Test Lactose or galactose (+) crystals and to the last carbon left side-up Fehling’s Test Confirmatory test for Glucose - - basis of DIL isomer Detects aldehydes & sugar alpha-Down Beta-up (+) brick red ppt G 6. Reaction w/ Phenyhydrazine (Osazone/Kowarsky test) sucrose/maltose so Lactose 7. Fermentation - anaerobic hydrolysis of carbohydrates glu/man/Fre g galactose st into simple alcohols & ketones by microorganisms 8. Reaction w/ alcohols: Acetal Formation PROTEINS CHON amino Acids - Polymers of amino acids linked by Peptide Bonds; CHON - Precipitated by Alcohol, Salts, & Inorganic Salts Enzymes Acting myosin - Uses: storage & transport, muscle contraction, biological Hormones Immunoglobulin (MADGE) catalyst, metabolic control, immune system Myoglobulin-carrier of oxygen Hemoglobin-carrier of oxygen - General test for proteins: Biuret test (+) violet Transferrin-transport of Iron *ISOMERISM* Ferritin-storage of Iron Isomers - compounds w/ same molecular formula, but *AMINO ACIDS: building blocks of proteins* different atomic arrangement Types of Isomers: Functional Isomers - differ in their physical properties Stereoisomers - different spatial arrangement of atoms. (3D) Geometrical or Cis-Trans Isomers (E-Z isomers) Tran's Optical Isomers lopposite is same ▪Dextrorotatry(+) rotate plane of polarized light to ___ Right enantiomers Characteristics: ▪ Levorotary(-) rotates plane of polarized light to ____ Left COOH NHG 1. Amphoteric - react chemically as either acid or base Anomers - difference resides in steric arrangement 2. Chiral/Optically Active Except: ______ Glycine chiral diff constituents a carbon is - I. about C1, β = _______, up α = ________ Down 3. Zwitter ions/Dipolar Ions Epimers - differ only in the configuration of a single - Isoelectric species - form of a molecule with equal positive & asymmetric carbon atom negative charges thus is electrically neutral. ▪D-glucose/ D-mannose = Epimers at ___ C2 - Isoelectric pH (pI) - pH midway between pKa values on ▪D-glucose/ D-galactose = Epimers at ___ [4 either side of isoelectric species neutral can be cation zwitterion anion acidic amino acid = ang of a lower plas Pit Low pl high pit P + pl = pl2 basic amino acid = aug of a higher plas  2 or more more than 1 polypeptide subunit NAME ABBREVIATIONS Notes Quaternary Structure - arrangement of polypeptide Amino Acids with Acidic Side Chains (Negatively Charged) chains in relation to one another in a multi-chained protein, Aspartic Acid Asp, D forming the overall protein structure; noncovalent bonds Glutamic Acid Glu, E Amino Acids with Basic Side Chains (Positively Charged) Hydrolysis - destruction of primary level of organization Common parts : N terminus Lysine Lys, K Denaturation - destruction of 4/3/2 levels of protein · · c terminus primary lang I X Residues (basic Kase) organization w/ loss of function Blue-main Arginine Arg, R ionic interaction Denaturants: (1) High temperature; (2) Extreme pH; Green-side Histidine His, H (3) Organic Solvent: mercapto ethanol B Amino Acids with Polar, Uncharged, Non-Ionic Side Chains Alcohol due to OH group (Hydroxyl) *CLASSIFICATIONS OF PROTEINS* Serine Ser, S Based on COMPOSITION: Threonine Thr, T A. Simple Proteins - consist only of a-amino acids Tyrosine Tyr, Y Examples: a. Albumin Egg albumin, Serum Albumin due to Amide groups b. Globulin Serum globulins, myoglobulin Aspargine Asn, N c. Prolamines Gliadin from Wheat, Zein from Corn Glutamine Gln, Q d. Glutelin glutelin from Wheat due to SH or Thiol group e. Scleroproteins Collagen, Elastin, Keratin Cysteine Cys, C f. Histones Histones due to H group g. Protamines Salmin & Sturin in Fish Sperm Glysine Gly, G B. Conjugated Proteins - amino acids naturally conjugated w/ nonprotein substances (Prosthetic group). Ex: Amino Acids with Nonpolar, Hydrophobic Side Chains mucoproteins, glycoproteins, lipoproteins, chromoproteins with Aliphatic R group Alanine Ala, A Based on 3D SHAPE or GROSS STRUCTURE: Leucine Leu, L Globular Proteins - water soluble Hgb protamines Insulin 1gb , , histones , Isoleucine Ile, I Water Saline Alcohol Acid/Base Valine Val, V Albumin Yes Yes Yes Yes Proline Pro, P Globulin No Yes Yes Yes with Aromatic Ring Prolamines No No Yes Yes Phenylalanine Phe, F Glutelins No No No Yes Tryptophan Trp, W Histones - basic proteins extracted from certain with Sulfur group glandular tissues e.g. thymus & pancreas Methionine Met, M Protamines - strongly basic, low MW proteins from General test for AAs: Ninhydrin test (+) violet (Except ______) PROLINE fish sperm cells. Ex: Salmin (salmon sperm) Phenylalanine Leucine *Protamine Sulfate - purified mixture of proteins from cannot be synthesized Essential (PVT TIM HALL) and Non-essential can be synthesized valin Tryptophan Lysine sperm/testes of species of fish (Oncorhyncus suckley) Ketogenic (LL), Glucogenic, or Both (FITTT) threonine Isoleucine Phenylalanine Isoleucine * Fibrous Proteins - water-insoluble; structure, protection methionine threonine tryptophan Collagen - most abundant proteins in mammals; Histidine tyrosine *LEVELS OF PROTEIN ORGANIZATION * Arginine a major protein of connective tissue in vertebrates; (connective skin tissue tendon, , Leucine Bloodels) , wrapping peptide Bonds Primary Structure - sequence of AAs in a polypeptide AA , contains hydroxylysine and hydroxyproline. chain; most important level since it determines overall shape, *Tropocollagen - basic unit of collagen; triple helix function & properties of protein; cannot be denatured Elastin - in tendons, ligaments, arteries, and other cannot be FYI: Sickle-cell anemia is caused by a genetic defect where elastic tissues infected in malaria Valine is changed to Glutamic Acid at one position. Keratin - contain large amounts of sulfur as alpha helix , beta folding pleated H bond , Secondary Structure - spatial arrangement of AAs in a cysteine; found in skin, wool, feathers, silk, nails hair , hooves polypeptide chain in repetitive patterns like the α-helix and β- Myosin - found in muscle tissue pleated sheet, stabilized by Hydrogen bonds Fibrinogen - found in blood, for blood clotting. R group intXn 3D Tertiary Structure - overall arrangement and Ex : fibrous & Globular interrelationship of various regions/domains, and individual Based on BIOLOGICAL FUNCTION: Proteins amino acid residues of a single polypeptide chain; 3D shape 1. Enzymes - biological catalysts important proteins most class of Hydrophobic Interaction of non polar side chains optimal activity at 35-40C, destroyed at >65C g H-bonding between polar amino acids retarded by heavy metals, formaldehyde, & I2 Ionic interactions between acidic & basic AAs 2. Hormones - proteins that regulate body processes 3. Storage Protein - nutrient stores Ex: Ferritin, Ovalbumin (eggs) Dipole-dipole Interaction between serine groups 4. Transport Proteins Function transport - Disulfide bonds between cysteines (curly hair) C SH) - 5. Structural Proteins - Ex: Keratin, Elastin, Collagen forms as organism structure  Antibodies - combine wh foreign proteins w/ gain access to BS that help fight infection Fibrinogen & thrombin - necessary in blood coagulation 6. Protective Proteins - Ex: Immunoglobulin *Enzyme commission (EC) number - based on classification 7. Contractile Proteins - Ex: Actin & Myosin major element in the contractile system of muscle 8. Toxic Protein - Ex: Snake venom, Botulinum toxin Defensive role for plants & *Enzyme kinetics reap. for blood animals poisoning Michaelis-Menten Model attacks same site highest ~ DERIVED PROTEINS slightly chemical/physical Proteins altered by means conc. reached -surmountable/reversible Primary Protein Derivatives - active site a. Proteans - insoluble products of action (for short -insurmountable /irreversible time) of water, dilute acid or enzymes. Ex: Fibrin - allosteric site b. Metaproteins/infraproteins - products of further action of acids/akalis. Ex: Acid/Alkali Albuminates rate of rx enzyme substrate complex c. Coagulated Proteins - insoluble products of action - of heat/alcohol. Ex: Coagulated Albumin, Cooked Meat Secondary Protein Derivatives: substrate conc. on half * MW: Proteoses>Peptones>Peptides Vmax subtrate concentration a. Proteoses - water-soluble, not coagulated by heat, pptd by saturating solutions w/ (NH4)2SO4 Lineweaver-Burke Plot b. Peptones -water soluble, not coagulated by heat, not pptd by saturating solutions w/ (NH4)2SO4 but by alkaloidal reagents (Phosphotungstic acid) c. Peptides - combination of two+ amino acids, Clowest ( carboxyl group bound to amino group of other vertical intersection *ENZYMES* parallel horizontal intersection protein part) (non ▪ Apoenzyme - protein part of enzyme w/o bound cofactor LIPIDS CHONP fatty Acids ▪ Holoenzyme - apoenzyme + bound cofactor; active form - water-insoluble organic subs; soluble in non-polar solvent ▪ Zymogen - inactive form. Ex: Pepsinogen Trypsinogen (chloroform, ether, methanol, hexane, & benzene); CHONP ▪ Substrate - molecule acted upon by an enzyme - uses: energy, structural, signaling, regulatory, auxiliary ▪ Cofactors - non protein substances requires for activity- secondary membrane,myelin steroid hormones culina cosmetics cell source secondary messengers , pharma , o -> Coenzyme/Cosubstrate - organic cofactors that dissociate I. Storage/ Neutral Lipids from the enzymes. Ex. NAD - vit B3, FAD - vit B2 A. Triglycerides/ Triacylglycerols (TAGs) of glycerol + FAC esters -> Prosthetic Group - inorganic cofactors that remain tightly 1. Saturated fatty acids - no double bonds bound to enzyme. Ex: metals (Fe, Cu, Mn, K, Mg, Se) # C Common Systematic Formula CnH2n+1COOH Classification of Enzymes (OTHLIL) 1 Formic Acid Methanoic Acid HCOOH 1. Oxidoreductases: catalyze redox reaction 2 Acetic Acid Ethanoic Acid CH3COOH ORD Subclasses: Oxidases. Reductases, Dehydrogenases 3 Propionic Propanoic Acid CH3CH2COOH 2. Transferases: catalyze transport of a functional group 4 Butyric Acid Butanoic Acid CH3(CH2)2COOH TAKP Subclasses: Transaminases (transfer amino group) 5 Valeric Acid Pentanoic Acid CH3(CH2)3COOH Kinases (/transfer of a phosphate group) 6 Caproic Acid Hexanoic Acid CH3(CH2)4COOH 3. Hydrolases: catalyze hydrolytic reaction or breaking of 8 Caprylic Acid Octanoic Acid CH3(CH2)6COOH bond via introduction of water 10 Capric Acid Deccanoic Acid CH3(CH2)8COOH LEPAND Subclasses: Lipases (hydrolyze ester groups in lipids) 12 Lauric Acid Dodecanoic CH3(CH2)10COOH Proteases (hydrolyze amide group in proteins) 14 Myristic Acid Tetradecanoic CH3(CH2)12COOH Nucleases (phosphate groups in nucleic acids) 16 Palmitic Acid Hexadecanoic CH3(CH2)14COOH 4. Lyases: catalyze non-hydrolytic cleavage; removal of 18 Stearic Acid Octadecanoic CH3(CH2)16COOH a functional group to form a double bond or breaking of a 20 Arachidic Eicosanoic Acid CH3(CH2)18COOH double bond by an interaction of a functional group 22 Behemic Acid Docosanoic CH3(CH2)20COOH Subclasses: Dehydrases (loss of water from substrate) Decarboxylase (loss of CO2 from substrate) 24 Lignoceric Tetracosanoic CH3(CH2)22COOH 5. Isomerase: intramolecular rearrangement of atoms Subclass: Epimerase - catalyze isomerization of chiral 1. Unsaturated fatty acids They bond have double center in substrate Ex: Racemase & Mutase —Monounsaturated (Monoenoic Acid) (one double bond): ▪ Palmitoleic Acid (16:19) ▪Oleic Acid (18:19) position of double bonds 6. Ligases: catalyze reactions joining 2 molecules no of carbons no of double bonds —Polyunsaturated (Polyenoic Acid):. Subclasses: Synthetases/synthase Carboxylases (forms bond between substrate & CO2) ▪ Linoleic Acid (18:29,12) ▪Linolenic (18:39,12,15) ▪Arachidonic Acid(20:45,8,11,14) Omega 3 -alpha linoleic Acid (ALA) Omega 6-linoleic Acid  *Phosphate Group - responsible for acidic character Reactions of Fatty Acids: *C2 - responsible for the difference between 2 nucleic acids. 1. Hydrogenation (double bonds to single) *Nitrogenous bases – purines & pyrimidines 2. Autooxidation (rancidification) fats air rancid leave to = 3. Sulfation (Metal acyl sulfate, i.e. detergent) 4. Saponification (Metal acylate, i.e. soap) 5. Epoxidation forming epoxy B. Waxes - esters of FAs w/ high MW monohydric alcohol. chain + FA II. Structural Lipid - major component of cell membrane replaced by A. Phosphoglycerides/Phospholipids – contain FAs, POy alcohol, and PO4. (Phosphatidic acid - parent cpd) cardiolipin a. Phosphatidylcholine (lecithin) Component cell mem. studied Ist b. Phosphatidylethanoloamine (Cephaline) blood clotting in ox heart CH3 reagent in VDRL c. Phosphatidylinositol secondary messenger *Rosenheim’s Test - detects Choline (+) White ppt B. Sphingolipids - sphingosine backbone and FAs, and cerebroside (ce mono) + Ganglioside (Ce Poly) + accessory groups; main lipid in brain tissue Sphingomyeline (Ce Poy Ceramide - parent compound, no accessory groups + ▪Nucleosides = nitrogenous base linked to a sugar. JUST FA choline) + C. Sterols - precursor in the synthesis of sex hormones ▪Nucleotides = building blocks (aka Nucleoside phosphate), composed of heterocyclic base, sugar, & phosphoric acid. III. Terpenoids Eicosanoids arachidonic Acid - - polymers of Isoprene Units; fat soluble vitamin (ADEK) DNA vs RNA Vitamin A - first fat-soluble vitamin discovered; essential in night blindness formation of rhodopsin & maintenance of normal retinal function, general antioxidant, maintains integrity of epithelial membranes Retinol = major natural form of Vitamin A * -orange Main Source: Carotenoids (carotenes, pro vitamin A) zeaxanthine & Lutein > - yellow (can be converted to Vit A) Lycopene red - ↓ = Bones Vitamin D - Calciferol; synthesized in skin through sunlight - 1. Ergocalciferol (Vit D2): plant steroid ergosterol 2. Colecalciferol (Vit D3): animal species 3. 7-Dehydrocholesterol: convert to calciferol on UV exposure Dihydrotachysterol synthetic - sub formed by reduction of tachysterol (closely related to engostura muscle weakness Vitamin E - prevents lipid peroxidation, antiaging vitamin - Rotation Clockwise Counter-clockwise bleeding Vitamin K - important in blood coagulation B-DNA - right handed; most common; Z-DNA - rare; left- Chemorrhage) ~ phosphate group hydrated form; 10 nucleotides/turn handed; 12 NUCLEIC ACIDS C1-10NP A-DNA - right handed; dehydrated nucleotides/turn; purines longer structure Nitrogenous : sugar : Deoxyribose XO H Pyrimidines ribose of shorter structures form; 11 nucleotides per turn most stable invitro storage Expression of genetic information DNA RNA *THE CENTRAL DOGMA* Function Carries genetic info Transmits genetic info he 1. Replication - DNA-directed DNA synthesis; Xerox/2 daughter strandr N-Base A, G T, C A,G U,C / 100 % “Semiconservative” & bidirectional accuracy dapat old Base Pairs A=T & G≡C A=U & G≡C 3 Phases: I new , Location Nucleus, Nucleus, Cytoplasm i. Initiation single strand binding proteins DNA - Unwound mitochondria - recognition of origin of replication Structure Double-Helix Single-stranded - Helicases: unwind double stranded-DNA Watson Crick Model molecule, shorter chain - DNA gyrase/Topoisomerase: relievesupercoiling of nucleotides - Primase: introduces the RNA primer (5-10 nucleotides) Propagation self-replicating synthesized from DNA ii. Elongation - from 5’ to 3’ end of the new strand when needed - DNA polymerases Levels of Primary to Primary & Secondary I - only one to remove DNA primers Organization Quaternary II - involved in DNA repair (N glycosidic Bond III - fastest, synthesize Okazaki fragments Structure: Sugar + Nitrogenous base + PO4 *DNA ligase - joins the Okazaki fragments (100-200 nucleotides) to be joined by DNA ligase Nucleoside left leading strand-synthesized continuously by DNA polymerase Nucleotide right lagging strand-synthesized discontinuously by adding RNA primers = ozaki fragments Phosphoester bond Phosphoanhydride Bond-Bond betw other POy sugar + PO4 5 prime-phosphate 3 prime-hydroxyl Antiparallelism-strands run oppositely iii. Termination *Okazaki Fragments - discontinous stretches in w/c lagging METABOLISM strand is initially synthesized during DNA replication - sum total of many organic reactions that go on The Sequence of the Major Events in DNA Replication: cutdown Catabolism - breakdown of molecules 1. DNA double helix is unwound by helicases. Anabolism - assembly/synthesis of macromolecules 2. Primase makes RNA primer for each DNA strand. 3. DNA polymerase (at the replication fork) synthesizes DNA in 5’ to 3’ direction, creating leading & lagging strands. CARBOHYDRATE METABOLISM 4. DNA polymerase removes the RNA primer & fills the gaps between the Okazaki fragments. Glycolysis Glucose to Pyruvate 5. DNA ligase joins DNA fragments (Okazaki fragments) of Glycogenesis Glucose to Glycogen the lagging strand, creating a single DNA molecule. Glycogenolysis Glycogen to Glucose ~ lower Fidelity/accuracy Gluconeogenesis Non carbohydrate to Glucose 2. Transcription - DNA-directed RNA synthesis unidirectional Glucose - pyruvate 3 Phases + Post-transcriptional processes: ❖ GLYCOLYSIS (aka Embden-Meyerhof Pathway) i. Initiation - main pathway for the oxidation of glucose to 2 pyruvate, for - Recognition of promoter region, unwinding carbohydrate catabolism - Removal of sigma subunit (RNA Polymerase) - Location: cytoplasm / cytosol template: anti-sense strandii. Elongation: RNA polymerase (does not require - Yield: 7 ATP per molecule of glucose non-temp : sense strand primer, does not possess proof reading activity) - Irreversible steps: #1, #3, #10 important (rate-limiting) steps Kinase most - iii. Termination - 2 Stages/Phases: P - Rho-dependent: termination sequence use 1. Energy investment (steps 1-5) P - Rho-independent: palindrome sequence cloop) receiving 2. Energy pay-off (steps 6-10) Post-transcription: ▪ Capping - protects 5’ (______) head w/ 7-Methylguanine glucose ▪ Polyadenylation - Protects 3’ (___) tail w/ adenylyl groups HK · splicing - removing introns (non coding regions) & Keeping exons (coding regions) 66p 3. Translation - RNA-directed protein synthesis ribosomes occurs in Pol requires : mRNA-nucleus 3 Phases: tRNA-carry amino rRNA-ribosome itself acids FGP i.Initiation: Start Codon AUG (Kozak sequence in PFK eukaryotes, Shine-Dalgarno sequence in prokaryo) Fl6BP woble hypothesis : (aminoacyl)- charged site A tRNA enters ↓ tRNA recognize than one codon more ii.Elongation Site (peptidyl) peptide P (Exit/Empty) uncharged - bonds form Esite - tRNA exits DHAP Aldo iii.Termination: Stop codons UAG UGA UAA ↓ GLAP GLAP RULES OF THE GENETIC CODE 1 , 3 Bi I. Almost universal (except AUG, in prokaryotes: N- P6K formylmethionine) II. Degenerate/Redundant 3P6 III. Non-ambiguous PGM IV. Commaless 296 V. Non-overlapping Enolase MISTAKES HAPPEN! PEP Mutation = a change in the base sequence of DNA PK ▪ Nonsense mutation - substitution of bases Pyruate resulting in a nonsense codon, a termination codon uAG , UGA , UAA ▪ Missense mutation - substitution of basesAcid pyruvate-glucose glutamic resulting in an amino acid substitution in a protein & valine ❖ GLUCONEOGENESIS exact of glycolysis reverse - conversion of non-carbohydrates to glucose no effect ▪ Silent Mutation - substitution of bases resulting in - reverse of glycolysis except for the irreversible steps: a different codon that calls for the same amino acids #10: Pyruvate carboxylase & PEP carboxylase carboxykinase ▪ Point Mutations: #3: Fructose-1,6-bisphosphatase -Tranversion: purine replaces pyrimidine, or v.v. #1: Glucose-6-phosphatase -Transition: purine replaces purine -Insertion insertion of base -Deletion Deletion of base FRAME SHIFT MUTATION-sequence , biglang gumalaw yung buong pag read ng sequence  NADH para maalis hydrogen = DHAP > G3PD - , then HYG3P > - FADH2 take It with Gapp = G3P = DHAP *Shuttles: bring NADH to mitochondria to make ATP via ETC ❖ GLYCOGEN METABOLISM Glycogenesis & Glycogenolysis Product-63P DHAP-G3P-DHAP Enzyme-G3PD NADH-FADH2 to make aspartate : enzyme : aspartate amino transferase enzyme oxalo acetate Malate-IN > = NADH para alis H- malate get amino group from - to > oxaloacetate = enzyme a Keto-out glutamate and put on GLYCOGEN STORAGE DISEASES ↓ oxaloacetate = aspartate Type & Name Enzyme defective. glutamate In aspartate our - 0 Glycogen synthase 1 Von Gierke Glucose-6-phosphatase malate - in 2 Pompe’s a-Glucosidase aspartase-out 3 Cori’s Debranching enzyme glutamate-in a ketoglutarase-out 4 Andersen’s Branching enzyme receive amino group transporter work lang Kung may exchange = glutamate 5 McArdle’s Muscle phosphorylase small , not often seen or 6 Her’s Liver phosphorylase used 7 Tarui Phosphofructokinase ❖ KREB’S CYCLE AKA Citric acid cycle, TCA cycle cata & and - central hub of metabolism; amphibolic, intemediary generates cofactors - oxidation of AcetylCoa to 2 CO2 & generates cofactors: a-ketoglutarate - AA metabolism SuccinylCoA - heme synthesis ❖ PYRUVATE METABOLISM Oxaloacetate - role in gluconeogenesis using energy - Anaerobic via lactate dehydrogenase = Lactate (-2NADH) instead of - Location: mitochondrial matrix gaining (Anaerobic in microorganisms: alcoholic fermentation via