1-Why did the reactions with enzyme produce higher absorbance values than the reaction with out enzyme?...
- 1-Why did the reactions with enzyme produce higher absorbance values than the reaction with out enzyme?
- 2-what are the overall benefits of enzymes as catalysis.
Homework Answers
1. The rate of product formation increases with increasing substrate concentration. However, in the presence of enzymes the function dp/dt has higher values and a much steeper slope. This implies enzymes greatly increase the reaction rate. However, as the enzymes become saturated, the reaction rate levels off. That is why in the presence of enzymes the absorbance value is more than in its absence.
2.Most of the chemical reactions that take place within a cell involve protein catalysts called enzymes. Enzymes, like other catalysts, speed up the rates of chemical reactions by lowering the activation energy of that reaction (i.e., the amount of energy needed to start a chemical reaction).
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1-Why did the reactions with enzyme produce higher absorbance
values than the reaction with out enzyme?...
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1. The following kinetic data was generated for the Hst enzyme. The overall reaction for this...
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Which statement about enzyme catalysis is false? All of the active site amino acids are next to each other in the primary sequence. Enzymes speed up reactions by forming specific non-covalent bonds between the enzyme amino acids and the transition state molecule. Some enzymes require other molecules, called cofactors, to carry out chemical reactions. Generally, the most important amino acids for an enzyme's function are those in the active site. Question 6 1 pt When [S] is much more than...
1. The following kinetic data was generated for the Hst enzyme. The overall reaction for this enzyme is: OH ОН + NH3 NH2 All reactions are carried out in a final reaction volume of 2 mL with 0.1ug of purified Hst protein present at pH 7.8. The Hst protein has a molecular weight of 90 kDa based on estimates from gel filtration column chromatography and a molecular weight of 45 kDa based on estimates from denaturing SDS PAGE gel electrophoresis....
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( --/ Question 1 What is the incorrect statement about catalysis? The enzyme-substrate complex has lower free energy than the free substrate The stronger the enzyme-substrate interaction, the higher the Km value. At very high substrate concentrations, the reaction rate is independent of the substrate concentration. The enzyme-substrate complex is not the transition-state molecule. The higher the turnover number of a catalyst, the lower the catalyst concentration needed to reach a certain maximum reaction rate.
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