Enzymes act as catalysts in biochemical reactions.
Most catalysts are proteins.
Lower activation energy to accelerate reactions.
Activation energy= energy difference between ground and transition states.
Transition state involves breaking/forming bonds.
Enzymes are highly specific and regulate reaction rates under mild conditions.
Substrates are reactants in enzyme-catalyzed reactions.
Specificity: Enzymes selectively recognize substrates.
Fit between substrate and enzyme controls product formation.
Enzymes mediate virtually all cellular reactions.
Catalytic power is the ratio of enzyme-catalyzed to uncatalyzed rates.
Regulation ensures appropriate reaction rates based on cellular needs.
Cofactors: inorganic ions essential for enzyme function.
Coenzymes: organic molecules that carry functional groups, often derived from vitamins.
Kinetics examines reaction rates and factors affecting them (enzymes, substrates, temperature).
Vmax: maximum reaction velocity, theoretically asymptotic as substrate increases.
Km: Michaelis constant; a low Km indicates high affinity for substrates.
pH affects enzyme structure and activity; enzymes have various ionizable side chains.
Coenzymes and cofactors act as non-protein enzymes.
Transition state formation is crucial for enzymes to facilitate reactions.
Reversible inhibitors (non-covalently bound):
Competitive: binds the active site.
Uncompetitive: inhibits function without affecting substrate binding.
Mixed: affects both functions.
Irreversible inhibitors (covalently bound): often transition state analogs.
Regulation ensures metabolic reactions are suitable for cellular requirements.
Involves genetic regulation, allosteric modulation, and covalent modification.
Enzymes at key metabolic pathway steps are modulated by effectors.
Can be activators or inhibitors.
Isozymes are enzymes differing in subunits but performing similar functions.
Inactive enzyme precursors activated by proteolytic cleavage.
Fibrinogen (zymogen) converts to fibrin via thrombin.
Monosaccharides, disaccharides, polysaccharides defined.
Monosaccharides: simplest sugars.
Oligosaccharides: 2-10 sugar residues.
Polysaccharides: polymers of sugars.
Cyclization forms chiral centers (anomeric carbon).
Stereoisomers: same molecular formula, different spatial orientation.
Diastereomers: non-mirror image stereoisomers.
Epimers: differ at one chiral center.
Glycation: non-enzymatic glucose attachment.
Glycosylation: enzymatic glucose attachment.
Formed via dehydration reactions; various types exist (O, N, S, C).
Reversible under certain conditions (acidic/enzymatic hydrolysis).
Nonreducing sugars lack free OH on anomeric carbons.
Common nonreducing examples include sucrose.
Starch (amylose, amylopectin), glycogen, cellulose, chitin, hyaluronic acid, heparin defined.
Structural and energy storage roles.
Glycogen: linear a1→4 and branched a1→6 linkages.
Amylose has a1→4, amylopectin has a1→4 and a1→6 linkages.
Heparin (anticoagulant), hyaluronates (joint lub), chondroitins, dermatan sulfate.
Basic structure and classifications of fatty acids.
Saturated, mono-, polyunsaturated: natural state.
Identification via delta (Δ) and omega (ω) nomenclature.
Hydrocarbon chain length and saturation affect solubility/melting points.
Form through dehydrogenation; impact on health.
EFAs required through diet; n-6:n-3 ratio relevance in health.
TAGs as long-term energy sources, storage forms.
Cholesterol modulates membrane fluidity; physiological roles.
Barrier, transport, energy transduction functions detailed.
Amphipathic nature of lipids leads to formation of micelles, vesicles, and bilayers.
Structure and importance of phospholipids and sphingolipids.
Role in protein/lipid distribution across leaflets.
Membrane proteins and lipid motion dynamics explained.