TLS Online TPP Program

#Question id: 27962


Which of following is true regarding the Transketolase and Transaldolase
a. Transketolase catalyzes the transfer of a two-carbon fragment from a ketose donor to an aldose acceptor with TPP
b. Transketolase catalyzes the transfer of a three-carbon fragment from a ketose donor to an aldose acceptor with TPP
c. Transaldolase catalyses the transfer of a two-carbon fragment
d. Transaldolase catalyses the transfer of a three-carbon fragment

#Unit 1. Structure and Function of Biomolecules
  1. a and b
  2. b and c
  3. a and c
  4. a and d
More Questions
TLS Online TPP Program

#Question id: 620

#Unit 1. Structure and Function of Biomolecules

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

#Unit 1. Structure and Function of Biomolecules

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

#Unit 1. Structure and Function of Biomolecules

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

#Unit 1. Structure and Function of Biomolecules

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

TLS Online TPP Program

#Question id: 624

#Unit 1. Structure and Function of Biomolecules

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

#Unit 1. Structure and Function of Biomolecules

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