TLS Online TPP Program

#Question id: 10467


The COP1-SPA complex acts as a positive regulator as well as acts as negative regulator  by shown in statements;

a) Act as negative regulator−that targets transcription factors for degradation during phytochrome and cryptochrome responses

b) Acts as a positive regulator−that targets transcription factors for degradation during phytochrome and cryptochrome responses

c) Acts as a negative regulator− during UV-B signaling by interacting with the C-terminal region of UVR8 in the nucleus UVR8- COP1-SPA complex then activates the major transcription factor HY5, which controls the expression of many of the genes induced by UV-B

d) Acts as a positive regulator during UV-B signaling by interacting with the C-terminal region of UVR8 in the nucleus UVR8- COP1-SPA complex then activates the major transcription factor HY5, which controls the expression of many of the genes induced by UV-B

Whichof the following combination from avbove statements of UVR8 is true?

#Unit 6. System Physiology – Plant
  1. B and C
  2. A and D
  3. B and A
  4. A and C
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TLS Online TPP Program

#Question id: 645

#Unit 1. Molecules and their Interaction Relevant to Biology

Which of the following is the correct combination of marker enzymes used to identify different organelles during subcellular fractionation of eukaryotic tissue?

TLS Online TPP Program

#Question id: 644

#Unit 1. Molecules and their Interaction Relevant to Biology

Enzyme X and Enzyme Y are both involved in monosaccharide metabolism. Enzyme X uses glucose as a substrate while Enzyme Y uses fructose as a substrate. At pH=7.0, Enzyme X has a Vmax of 10 μM/s while Enzyme Y has a Vmax of 20 μM/s. Both enzymes have a Km of 3.0 mM for their respective substrates. Which aspects of its reaction will be changed by Enzyme Y?

TLS Online TPP Program

#Question id: 643

#Unit 1. Molecules and their Interaction Relevant to Biology

The hydrolysis of lactose is catalysed by b-galactosidase as given below

Which of the following could be correct mechanism for this hydrolysis reaction?

A. Nucleophilic attack by the carboxylate group of Glu/Asp on the C-1 carbon atom of the galactose moiety within glucose, releasing glucose and forming an intermediate with the galactose linked to the enzyme through an ester linkage. Water then attacks this carbon atom, displacing the glutamate carboxylate and releasing galactose.

B. Electrophilic attack by the carboxylate group of Glu/Asp on the C-1 carbon atom of the galactose moiety within glucose, releasing glucose and forming an intermediate with the galactose linked to the enzyme through an ester linkage. Water then attacks this carbon atom, displacing the glutamate carboxylate and releasing galactose.

C. Nucleophilic attack by the carboxylate group of Lys/Arg/His or bivalent cation on the C-1 carbon atom of the galactose moiety within glucose, releasing glucose and forming an intermediate with the galactose linked to the enzyme through an ester linkage. Water then attacks this carbon atom, displacing the glutamate carboxylate and releasing galactose.

TLS Online TPP Program

#Question id: 642

#Unit 1. Molecules and their Interaction Relevant to Biology

The graphs P, Q and R show the variation of rate constant (k) with temperature. The reactions represented by P, Q and R, respectively, are

TLS Online TPP Program

#Question id: 641

#Unit 1. Molecules and their Interaction Relevant to Biology

Which of the following does NOT describe a mechanism that cells use to regulate enzyme activities?

A. Cells control enzyme activity by phosphorylation and dephosphorylation.

B. Cells control enzyme activity by the binding of small molecules.

C. Cells control the rates of diffusion of substrates to enzymes.

D. Cells control the rates of enzyme degradation.

E. Cells control the rates of enzyme synthesis.

F. Cells control the targeting of enzymes to specific organelles. 

TLS Online TPP Program

#Question id: 640

#Unit 1. Molecules and their Interaction Relevant to Biology

The data in the table above were collected for an enzyme-catalyzed reaction. The Km for this enzyme is approximately