Metabolismo y vías metabólicas, Esquemas y mapas conceptuales de Biología

¡Descarga Metabolismo y vías metabólicas y más Esquemas y mapas conceptuales en PDF de Biología solo en Docsity! METABOLISM Metabolic Pathways Anabolic: consumes energy building molecules Catabolic: Breaks down molecules, making energy available Energy Kinetic: motion of objects Potential: matter's energy as a resut of location and structure Thermal energy: random movement of atoms and molecules Chemical energy: available for chemical reactions Thermodynamics Energy can be transferred and transformed, but it cannot be created or destroyed. Every energy transfer or transformation increases the entropy of the universe Spontaneous process: no energy, so increases entropy, and decreases free energy Nonspontaneous: uses energy, so decreases entropy *Entropy: measurement on how much energy is dispersed in a system Free energy (G): can perform when temperature and pressure are uniform Stability: unstable systems have higher G, and stable lower G. The system always looks to lower down G Equilibrium: G increases when there is no equilibrium. Chemical Reactions Exergonic: breaks down molecules, so energy goes otuward Endergonic: builds molecules so energy goes inward Energy coupling: ATP is responsible for using the released energy from the exergonic reactions to drive endergonic ones. ATP: releases free energy when hydrolyzed, turning into ADP, and allowing endergonic reactions Enzymes Activation energy barrier: Catalysis Denarturing Regulation of enzyme activity Enzymes lower the activation energy barrier and the transition state to speed up the reaction. The active site can provide a template or a more conductive microenvironment. The enzyme may stretch or bend toward the transition state form Covalent bonding between the amino acid and the substrate Enzymes speed up a reaction, and can also reverse it. Active site: formed by some enzyme's amino acids, perform induced fit to attach a substrate. Enzyme-substrate complex: changed shpe of the shape during catalysis. Rate of enzymatic reaction increases when higher temperature, but extreme heat kills the cell Optional pH values are between 6-8, but each enzyme works in their own acidic or basic environments. Cofactors and coenzymes: helps the reaction take place Inhibitors Competitive: blocks the active site by entering it. Allosteric: binds to a allosteric site in the enzyme, changing its shape. The allosteric activator changes the catalycally shape and the inhibitor stabilizes the inactive shape. Cooperativity: shape change in 1 subunit is transmitted to the other subunits to allow more substrate attachment. Feedback inhibition: the end of the product acts as an inhibitor within the pathway. Allosteric regulation Location Multi-enzyme complex: product becomes substrate Structural components of particular membranes Within organelles with internal chemical environment By: Laura Ospina