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Unit 2.2 Enzymes: a Special Class of Proteins. Vocabulary:. Activation Energy : the amount of energy needed to get a reaction started. Enzyme : a special class of proteins that catalyze reactions in living organisms.
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Vocabulary: Activation Energy: the amount of energy needed to get a reaction started. Enzyme: a special class of proteins that catalyze reactions in living organisms. Catalyst: a substance that increases the rate of a reaction without being consumed as part of the reaction. Active site: part of an enzyme where a rxn occurs. Substrate: molecule(s) on which an enzyme acts. Denature: to deform or change the shape of, thereby rendering the enzyme inactive.
I. Reactions: (abbreviated as “rxn”) catalyst • General reaction equation: reactant(s) product(s) • Reactant(s): • Reactants are the substance(s) that are “doing the reacting”; usually written on the left side of the equation/arrow. • Product(s): • Products are the substance(s) “produced” as part of the reaction; usually written on the right side of the equation/arrow. • Catalyst: • Any substance that speeds up a rxn without being consumed as part of the rxn. • If a catalyst is used, it is written above the arrow to show that it is not consumed as part of the reaction.
Energy of Reactions: • Exergonic/Exothermic • exo = out, off; erg- = energy; therm = heat • Release energy • **Starting reactants have more energy than ending products** • Like a ball rolling downhill • Endergonic/ Endothermic • endo = in • Require/take in energy • **Starting reactants have less energy than ending products** • Like pushing a ball uphill
Activation Energy: amount of energy needed to start a reaction • Even if reaction is exergonic, may need energy to start. • Catalysts reduce activation energy: • Make reactions happen much faster, but are not consumed as part of the reaction, so can be reused again and again. • Enzymes are biological catalysts.
“A” represents activation energy needed for rxn. • “B” represents activation energy needed when a catalyst is available (same reaction, less activation energy). • Is this rxnendergonic or exergonic?
II. Enzymes • An enzyme is a protein whose function is to catalyze chemical reactions • Enzyme names end in “-ase” • Enzymes can be named for substrate on which they act: • Ex: lactase breaks down lactose; peroxidase breaks down peroxide • Or the type of reaction that the enzyme catalyzes: • Ex: DNA polymerase forms DNA polymers
Structure of enzymes: • Active site has specific fit for substrate • Like a “lock-and-key” • Substrate: molecule(s) that an enzyme breaks apart or puts together • Active site: area of enzyme that interacts with substrate
Enzymes reduce activation energy in two ways: • Holding substrate in correct orientation to make joining, bonding easier • Or may “twist” substrate to make breaking bonds easier
IV. Speed of Reaction: • Three factors can change how fast a reaction occurs: • Amount of substrate • More substrate = faster rxn, until enzyme is working as fast as possible • Less substrate = slower rxn • Amount of enzyme • More enzyme = more rxns • Less enzyme = fewer rxns
Temperature • As temp. decreases, then rxn slows down - why? • lower temp = less energy, so molecules have less energy, move more slowly • As temp. increases, then rxn speeds up – why? • higher temp = more energy, so molecules have more energy, move more quickly • But if temp. is too high, then “denatures” enzyme • Denature = deformed, changes shape of active site so substrate no longer fits
V. Factors that affect enzyme function • Enzymes need correct conditions to keep correct shape: • Temperature: depends on organism • ~95-101°F for warm-blooded animals • pH: depends on the enzyme • Stomach enzymes need low pH (~2) • Intestinal enzymes need high pH (~8) • Amount of salt: depends on cell chemistry • Most need low salts (0.1M) • But halophilic algae/bacteria can stand higher amounts
If conditions are not correct, then enzyme can deform - denature. • High temperatures: break hydrogen bonds that hold polypeptide chains together • Wrong pH: can change charge (+/-) of amino acids, deforms them • Too much salt: can change ionic interactions of amino acids, cause them to deform