TLS Online TPP Program

#Question id: 603


Nonclassical competitive inhibition involves ________.

#SCPH05 I Biotechnology
  1. binding of the substrate at both the active site and at the inhibitor site

  2. binding of either the substrate to the active site or the inhibitor to its own binding site thus preventing the other from binding

  3. binding of the inhibitor to the substrate followed by binding of this complex to the active site

  4. chemical removal of the substrate from the active site by reaction with the inhibitor

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TLS Online TPP Program

#Question id: 620

#SCPH05 I Biotechnology

Which of the following statements about a plot of V0 vs. [S] for an enzyme that follows Michaelis-Menten kinetics is false?

TLS Online TPP Program

#Question id: 621

#SCPH05 I Biotechnology

Michaelis and Menten assumed that the overall reaction for an enzyme-catalyzed reaction could be written as Using this reaction, the rate of breakdown of the enzyme-substrate complex can be described by the expression:

TLS Online TPP Program

#Question id: 622

#SCPH05 I Biotechnology

An enzyme-catalyzed reaction was carried out with the substrate concentration initially a thousand times greater than the Km for that substrate.  After 9 minutes, 1% of the substrate had been converted to product, and the amount of product formed in the reaction mixture was 12 micromol.  If, in a separate experiment, one-third as much enzyme and twice as much substrate had been combined, how long would it take for the same amount (12 micromol) of product to be formed?

TLS Online TPP Program

#Question id: 623

#SCPH05 I Biotechnology

Which of these statements about enzyme-catalyzed reactions is false?

TLS Online TPP Program

#Question id: 624

#SCPH05 I Biotechnology

The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: The Km for this enzyme is approximately:

TLS Online TPP Program

#Question id: 625

#SCPH05 I Biotechnology

For enzymes in which the slowest (rate-limiting) step is the reaction Km becomes equivalent to: