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