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homeostasis constancy of the body's internal environment by means of self-regulation
enzyme - a protein molecule that functions as an organic catalyst:(speeds up reactions by lowering the energy of activation) - molecules that control metabolism
metabolism all the chemical changes that occur within a cell that maintain homeostasis
substrate - reactant in a reaction controlled by an enzyme
energy of activation energy that must be added to cause molecules to react with one another
cofactor an inorganic ion (often minerals minerals) or an organic non-protein:("coenzyme") that helps enzymes to function properly
coenzyme organic non-protein molecule that aids the action of the enzyme (to which it is loosely bound) - usually derived from vitamins
vitamin small organic molecules required in our diet (in small amounts) for synthesis of coenzymes
metabolic pathways step-wise series of chemical reactions from the initial REACTANTS to the final PRODUCTS
how do most enzymes get their names? named after their substrates
three important characteristics of an enzyme: - function is to speed up reaction rates - act specifically with only one or more reactant(s) [aka substrate(s)]
the place where the substrate actually binds on the enzyme is called the _____, and has a specific ______ that allows the substrate to bind - active site - geometric shape
the substrate enters the active site & the enzyme helps complete the reaction, which is either ______ or ______ - "ANA"bolism (synthesizing / joining together) - "CATA"bolism (breaking bonds)
apoenzyme the protein part of an enzyme
the apoezyme may be inactive until joined by a ______. In many cases, the enzyme consists of the protein and a combination of one or more of these. (this enzyme complex is usually called just "the enzyme") cofactor
describe: (1) lock and key theory (2) induced fit theory (1) substrate fits EXACTLY into enzyme's active site. 1 type of substrate for every enzyme. If wrong shape, then no reaction (2) active site is a bit flexible--adjusts to molds itself around substrate. Still only bonds to a specific substrate
activation energy energy that must be supplied to cause molecules to react with each other. Enzymes lower this energy by bringing molecules closer together & holding them there while reaction takes place
factors affecting enzyme activity: (detail on written sheet) - pH - temperature ( > 40° C = denatured) - concentrations of substrate - concentration of enzyme
enzyme inhibitors molecules that interact with the enzyme to prevent it from working normally (eg: drugs & poisons)
competitive inhibitors inhibitor closely resembles the substrate--enters active site, preventing actual substrate from going in - USUALLY REVERSIBLE
non-competitive inhibitors inhibitor bonds near or away from active site--modifies structure of the enzyme and active site so the substrate cannot fit
allosteric inhibition type of non-competitive inhibition--inhibitor binds at a site away from the active site, changing the structure so that the substrate doesn't fit (eg: metals bonding -- IRREVERSIBLE denatures or deactivates them)
Created by: Alyssa_bas