What two important properties of an enzyme can be determined from the graph shown below?    1. An indication of the affinity an enzyme has for its substrate  2. The total amount of product produced at the end of the reaction  3. The number of substrate molecules that can be converted into product per unit time  4. The difference in free energy between the products and the substrates  5. The difference in free energy between the transition state and the substratesGroup of answer choices1 and 21 and 34 and 51 and 42 and 3 PreviousNext

Which feature explains the specificity of an enzyme?

Consider the graphs below, showing the energy profile through the same reaction under different conditions. What has changed in condition B compared to condition A?Group of answer choicesMore substrate has been added.More product is being formed.The reaction has become unfavourable.An enzyme has been added.An enzyme has been taken away.

Make different graphs 4 the effect of Temperature, pH, Substrate concentrations on enzymes

1. TRUE regarding enzymes: Enzymes are proteins Enzymes are specific Enzymes are also called biological catalysts All of the above__ 2. Where will the substrate bind in an enzyme to proceed an enzyme reaction? Active site Allosteric site Alternative site All of the above__ 3. Inorganic molecules that are essential for enzymatic activity is called: Cofactors Coenzymes Isoenzymes All of the above__ 4. Which of the following are coenzymes? Zn2+ NAD ATP All of the above__ 5. What equation can be used to describe enzyme kinetics? Beers Law Equation Michaelis-Menten Equation Henderson-Hasselbach Equation None of the above__ 6. Which of the following refers to the Michaelis conastant? Km Substrate concentration at 1⁄2 Vmax Either Neither__ 7. What type of enzyme inhibition causes conformational changes in the active site of an enzyme? Competitive inhibition Non-competitive inhibition Uncompetitive inhibition __ 8. Competitive inhibition causes what change to Michaelis constant? Unchanged Increase Decrease None of the above__ 9. Zymogens are: Inactive enzymes Active enzymes

Enzyme A catalyzes the conversion of substrate S to product P.  When enzyme A is phosphorylated, its kcat value changes from 10 s−1 to 5 s−1 and its KM value changes from 100 μM to 20 μM.  If equal concentrations of each enzyme form are used then compared to the unphosphorylated enzyme A, the phosphorylated form:A.has a higher catalytic efficiency and yields a faster reaction rate when [S] < 20 μM.B.has a higher turnover number and yields a faster reaction rate under saturating conditions.C.has a lower affinity for S and yields a slower reaction rate at all [S].D.is allosterically inhibited and yields a lower reaction rate at all [S].