Enzymes
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| enzymes can catalyze a biochemical reaction without? | altering the equilibrium point of the reaction,being consumed,changing its composition
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| Active site | cavity where substrate is acted on
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| substrate | substance enzymes act upon
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| allosteric site | site that bind regulator
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| Iso enzyme | different forms of enzymes
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| cofactor | nonprotein enzyme activator
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| prosthetic group | enzyme/coenzyme complex
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| Nomenclature | numerical code, last number specific to each enzyme
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| activation energy | the energy necessary to begin the catalytic mechanism
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| how is activation energy achieved? | increased body temp, enzymes lower activation energy needed
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| name 4 catalytic mechanisms | absolute specificity, group specificity, bond specificity, stereosometric specificity
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| absolute specificity | enzyme combines with only one substrate and only one reaction occurs
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| group specificity | enzyme combines with all substrate in a chemical group
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| bond specificity | enzymes that are specific for certain chemical bonds
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| stereoisometric specificity | enzymes that predominantly combine with one optical isomer of a certain compound
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| factors that influence reactions | substrate concentration,enzyme concentration, pH, temperature, cofactors, inhibitors
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| at low concentrations reaction rate is directly proportional to the concentration of substrate | First order kinetics
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| substrate concentration is high enough to saturate all the available enzyme | zero order kinetics
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| what is the reaction rates for zero order kinetics | reaches plateau, becomes constant, independent of substrate concentration, only dependent on concentration of enzyme
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| Michaelic-Menton Constant(Km) | the constant from a specific enzyme reaction vs. the substrate concentration.
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| determined by plotting the rate of reaction of an enzyme catalysed reaction vs. the substrate concentration | Michaelic-Menten Constant (Km)
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| How does the enzyme concentration influence reactions | rate of catalyzed reaction
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| How does the pH influence the reaction? | denaturation or changes
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| How does the temperature influence the rate of reaction? | denaturation, rate
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| how does the cofactors influence the reaction? | necessary for reaction, excess-inhibit reaction
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| How does the inhibitors influence the reaction? | a substance that bind to particular enymes, resluting in a decrease in reaction velocity, 3 types
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| competitive inhibitors | bind to the active site and compete with substrate for the active site, may damage enzyme,
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| How may competitive inhibitors be overcome? | increase in substrate, but results in a higher Km, because increased substrate is required to react the max.catalysis
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| Non competitive inhibitors | bind the enzyme on a site other than active site, may be reversible or irreversible if the inhibitor destroys part of enzyme.cannot be be overcome by substrate
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| Uncompetitive Inhibitors | the inhibitor binds to the ES complex, the more ES compexes the more inhibition.
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| Increasing substrate will not overcome the problem but actually increase the problem | Uncompetitive Inhibitors
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| Enzymes are in very small quantities, so how are they measured? | measure activity to quantify enzyme concentrations
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| what are the 3 phases of reactions | lag, linear, substrate depletion
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| Lag phase | initial mixing of specimen and reagent, little change noted
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| Linear phase | zero order kinetic prevails, absorbance change becomes constant over time
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| Substrate depletion | dependant on the amount and activity of the enzyme present in the specimen
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| 1U | the amoount of enzyme tht will catalyze the reaction of 1 microole of substrate per minute under specified conditions of temp.,pH, substrate and activators
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| what does photometric measure? | increase product conc, decreased substrate conc.,decreased coenzyme conc.,increase conc. of altered coenzyme.
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| what does Mass Assay measure? | protein mass=enzyme concentration,
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| What is Mass Assay used for? | Isoenzyme
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| What has the Mass Assay replace? | Electrophoresis
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