spontaneous chemical reactions occur without a need for outside energy but may be very slow free...
DESCRIPTION
Every chemical reaction between molecules involves bond breaking and bond forming Free energy of activation, or activation energy (E A ): initial investment of energy to start the reaction Transition state: the summit where the reactants are in an unstable condition AB + CD AC + BD (SPONTANEOUS EXERGONIC)TRANSCRIPT
CHAPTER8.4ENZYMES AND
METABOLIC REACTIONS
Enzymes speed up metabolic reactions by lowering energy barriers
Spontaneous chemical reactions occur without a need for outside energy but may be very slow
Free energy: ΔG Catalyst: a chemical agent that
speeds up a reaction without being consumed by the reaction
Enzyme: a catalytic protein
The activation energy barrier Every chemical reaction
between molecules involves bond breaking and bond forming
Free energy of activation, or activation energy (EA): initial investment of energy to start the reaction
Transition state: the summit where the reactants are in an unstable condition
AB + CD AC + BD (SPONTANEOUS EXERGONIC)
How enzymes lower the ea barrier
Enzymes are proteins which are biological catalysts Speed up reactions by lowering the EA barrier
Heat denatures proteins and kills cells and it would speed up ALL reactions, so organisms need alternative- catalysis
Enzymes catalyze reactionsby lowering the EA barrier, Enabling the reactant moleculesto absorb enough energy to reach the transition state
Substrate specificity of enzymes
Substrate: the reactant an enzyme acts on
Enzyme-substrate complex: formed by an enzyme binding to its substrate
Enzymes + Enzyme-substrate Enzyme + Product(s)Substrate(s) complex
Enzymes=proteins=macromolecules
Substrate Specificity Active site: the restricted region of the
enzyme molecule that binds to the substrate a pocket on the surface of the protein
Induced fit: when the enzyme changes shape slightly so that the active site fits more snugly around the substance Brings chemical groups of the active site into
positions that enhance their ability to catalyze the chemical reaction
Catalysis in the enzyme’s active site
In most enzymatic reactions, substrate binds to active site and is held there by weak interactions
Side chains (R groups) of a few of the amino acids that make up the active site catalyze the conversion of substrate to product
Product departs Repeats Most metabolic reactions are reversible and an
enzyme can catalyze both forwards and backwards
The active site can lower an EA barrier by orienting substrates correctly, straining their bonds, providing a favorable microenvironment, and covalently bonding with a substrate
effects of local conditions on enzyme activity
Each enzyme has an optimal temperature and pH (6-8)
Cofactors: nonprotein helpers for catalytic activity required by many enzymes
coenzyme: if the cofactor is an organic molecule
http://www.youtube.com/watch?v=5eBzLgleVL8
Enzyme Inhibitors Inhibitors reduce enzyme function If done by covalent bonds the effects are
irreversible. Most are weaker bonds making them reversible Competitive inhibitor: binds to active site,
reduces productivity of enzymes by blocking substrates from entering active sites
- can be overcome increase [ ] of the substrate Noncompetitive inhibitor: impede reactions
by binding to different site on enzyme
8.5REGULATION OF
ENZYME ACTIVITY HELPS
CONTROL METABOLISM
Allosteric regulation of enzymes Allosteric regulation: any case where a
protein’s function at one site is affected by the binding of a regulatory molecule to a separate site - results in either inhibition or stimulation of activity
Cooperativity: mechanism that amplifies the response of enzymes to substrates
Feedback inhibition: a metabolic pathway is switched off by the inhibitory binding of its end product to an enzyme that acts early in the pathway
Ex: thermostat
Specific localization of enzymes within the cell
Some enzymes are grouped into complexes
Some are transported into membranes Others are contained inside organelles
Metabolism (intersecting set of chemical pathways characteristic of life)= choreographed interplay of thousands of different kinds of cellular moleculeshttp://www.youtube.com/watch?v=2N-ydg4J4tA
http://www.youtube.com/watch?v=M5bftq-W2aY
Works cited http://
www.uic.edu/classes/bios/bios100/lecturesf04am/lect04.htm
http://www.youtube.com/watch?v=5eBzLgleVL8
http://www.youtube.com/watch?v=2N-ydg4J4tA
http://courses.washington.edu/conj/protein/proregulate.htm
http://bio1152.nicerweb.com/Locked/media/ch08/