Enzymes and Kinetics

Related BrainMass Solutions

• Enzymes, Energy, and Catalysis

  The Kinetics of an allosteric enzymes: Allosteric enzymes Enzymes with multiple subunits have quarternary structure. One consequence of multiple subunits is that individual catalytic subunits each have their own active site.

• You characterize a new enzyme's kinetics.

  Reference: http://www.mrothery.co.uk/enzymes/enzymenotes.htm The solution provides detailed explanations and answer for the problem.

• Enzymes and Reaction Catalysis

  Assuming that Michaelis-Menten kinetics are followed, what will be the reaction velocity when the concentration of S is a) 1 x 10-5 M and b) 1 x 10-6 M. The MM equation is: V0 = (Vmax.

• Discussing Enzyme Proteins

  Catalysts do not change the thermodynamics of reactions (i.e. they don't alter the delta-G, for example), but they do change the kinetics of a reaction. Enzymes speed up reactions by changing the kinetics of a reaction. How do they speed them up?

• Enzyme Kinetics

  9202 Enzyme Kinetics The enzyme succinoxidase adds oxygen to succinate to give fumarate. The reaction follows Michaelis-Menton kinetics.

• Molecular Biology Questions

  The main difference between riboenzymes and enzymes is that enzymes use amino acids and riboenymes use nucleotides. 7. AU-rich elements are most commonly used in eukaryotes and are bound to many different transcripts. 8. True 9.

• On Energy

  By reducing the activation energy, the reactions are able to proceed at a more rapid pace, i.e. enzymes affect reaction kinetics, not their thermodynamics. ATP is considered a short-term form of energy for a cell.

• Enzyme Action

  6) Is it true that all enzymes are irreversibly inhibited at about 40C and that they are denatured at pH 3.0 and that a change in the pH of the environment will cause hydrolysis of the polypeptide of an enzyme and that enzymes have an optimum pH at which

• Inhibitors: Irreversible and Reversible

  Once all of the inhibitor is used up and a lot of the enzyme has been inactivated, then any further enzyme in the reaction will catalyze the reaction at the same basic kinetics as the control.