Answer Happy

1 kcat-keat Km-K kcat/Km-kat/Km Vmax Vmax Km/Vmax KVmax 1/Vmax=1/Vmax At At AO-Ao 1.5 points Select the best match to each of the listed items. Uncompetitive inhibition Competitive inhibition. Noncompetitive inhibition Exhibits zero order kinetics in an enzyme catalyzed reaction Slope in a Lineweaver-Burke Plot First order kinetics Km kcat y-Intercept in a Lineweaver-Burke Plot kcat/km substrate concentration is zero molar. turnover number Km/Vmax plot of InAt vs. tis linear plot of At vs. t is linear substrate concentration needed to obtain rate that equal to 1/2 Vmax only exhibits intercept effect in the Lineweaver-Burke plot saturating levels of substrate concentration > 5
keat kat Km-K kcat/Km-kat/K Vmax-Vimax Km/Vmax-KNmax 1/Vmax-1/Vmax At-A₂ AO-A₂ 1.5 points Select the best match to each of the listed items. Uncompetitive inhibition Competitive inhibition Noncompetitive inhibition Exhibits zero order kinetics in an enzyme catalyzed reaction Slope in a Lineweaver-Burke Plot First order kinetics Km kcat y-Intercept in a Lineweaver-Burke Plot kcat/Km exhibits both slope and intercept effects in the Lineweaver- Burke plot 1/At-1/AOkt plot of 1/At vs. tis linear catalytic enzyme/substrate rate constant Measure of substrate/enzyme binding affinity enzyme concentration needed to obtain rate that equal to 1/2 Vmax catalytic efficiency 1/Vmax
kcat keat Km-Km kcat/Km-kat/Km Vmax Vax Km/Vmax-Km/max 1/Vmax=1/Nmax At-A AO-Ao 1.5 points Select the best match to each of the listed items. Uncompetitive inhibition Competitive inhibition Noncompetitive inhibition Exhibits zero order kinetics in an enzyme catalyzed reaction i Slope in a Lineweaver-Burke Plot First order kinetics Km kcat y-Intercept in a Lineweaver-Burke Plot kcat/Km plot of 1/At vs. t is linear catalytic enzyme/substrate rate constant Measure of substrate/enzyme binding affinity enzyme concentration needed to obtain rate that equal to 1/2 Vmax catalytic efficiency 1/Vmax only exhibits slope effect in the Lineweaver-Burke plot At-AO-kt #