Michaelis menten equation - Samenvattingen en Aantekeningen
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In addition to the basic ES intermediate in an enzyme reaction, what other 
types of intermediates are formed and why are these intermediates so 
important? - Transition states occur in enzyme reactions that are 
important in product stabilization and changes in energy. 
Why would researchers try to determine the initial rate of enzyme activity 
(V0) at a very early time point in the reaction? What happens later in the 
reaction? W...
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Dephosporylation by a phosphatase requires each of the following except: 
-ATP 
-Water 
-Mg2+ - ATP 
Outline the roles of protein kinases, protein phosphatases, and of regulatory and hormonal and second 
messengers in regulating metabolic processes through covalent and allosteric interactions. 
During competitive inhibition, Km is__________. 
-Increased 
-Decreased 
-Unchanged 
-Unsaturated - Increased 
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Michaelis- Menten Equation - answerThe velocity of an enzyme reaction (V) is equal to the 
maximum reaction velocity (Vmax) times the substrate concentration (S) divided by substrate 
concentration plus the Michaelis constant ( Km) 
increases - answerRate of product formation ____________ as the initial substrate 
concentration is raised. 
Velocity - answerHow rapidly p...
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Describe the concept of mass action - Answers In chemistry, the law of mass action is the propo- sition that the rate of a chemical reaction is directly proportional to the product of the activities or concentrations of the reactants. It explains and predicts behaviours of solutions in dynamic equilibrium. 
Michaelis-Menten equation - Answers v = (vmax [S])/(Km + [S]) 
Key assumption in the Michaelis...
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What is the role of zinc in enzyme function? 
 Zinc acts as a cofactor, stabilizing the structure of enzymes and aiding in catalysis. 
 
Which type of bond forms between the amino group of one amino acid and the carboxyl group of 
another? 
 
 A peptide bond forms between the amino and carboxyl groups, linking amino acids together. 
 
How do enzymes use the lock-and-key model to explain substrate binding? 
 The lock-and-key model ...
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van der Waals interaction - Answers The ____________ describes the relation between interatomic distances, electronic charge, solution dielectric and free energies 
protein quaternary structure - Answers ____________ defines the relation among subunits in a multisubunit lattice 
protein primary structure - Answers ____________ defines the amino acid sequence 
protein secondary structure - Answers ____________ defines the motifs form...
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What is the primary function of enzymes? - Answers to catalyze all metabolic processes within a cell 
3 reasons why enzymes are necessary - Answers 1) reactions must be biologically friendly 2) reactions must be specific 3) reactions must have very high reaction rates 
What is the defective enzyme for Albinism? - Answers Tyrosine 3-monooxygenase (tyrosinase) 
What is the defective enzyme for Alkaptonuria? - Answers Homogentisate 1,2-dioxyge...
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Why does a plot of V vs S taper off and eventually reach a plateau at 
higher S levels? - - When S levels are high, the M-M plot actually 
approaches a limiting value of Vmax. 
- At high (S), where V approximates Vmax, virtually all of the enzyme active 
sites are occupied by substrate. 
- The addition of more S would not significantly increase the rate of 
reaction, because the rate of reaction is limited by the total active s...
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Describe the application of linear forms of the Michaelis-Menten equation to estimate Km and 
Vmax. 
Contrast the effects of an increasing concentration of substrate on the kinetics of simple 
competitive and noncompetitive inhibition. 
In utilizing the Michaelis-Menten equation, velocity (vi) and the Michaelis constant (Km) are 
_________-related. 
-Inversely 
-Directly 
-Equally 
-Proportionally Inversely
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Which of the following statements about the nature of enzyme catalysis is correct? - Answers d) An enzyme greatly accelerates reaction rates by lowering the activation energy of a chemical reaction. 
2. Which of the following statements about Michaelis-Menten enzyme kinetics is correct? - Answers d) Km, the Michaelis constant, reflects the (apparent) affinity the enzyme has for its substrate. 
3. Which of t...
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