TLS Online TPP Program

#Question id: 21250


A 56-year-old female was diagnosed with a tumor near the base of the skull, impinging on her optic tract. Which of the following statements about the central visual pathway is correct?

#Unit 7. System Physiology – Animal
  1. The fibers from each temporal hemiretina decussate in the optic chiasm, so that the fibers in the optic tracts are those from the temporal half of one retina and the nasal half of the other
  2. In the geniculate body, the fibers from the nasal half of one retina and the temporal half of the other synapse on the cells whose axons form the geniculocalcarine tract.
  3. Layers 2 and 3 of the visual cortex contain clusters of cells called globs that contain a high concentration of cytochrome oxidase.
  4. Complex cells have a preferred orientation of a linear stimulus and, compared to simple cells, are more dependent on the location of the stimulus within the visual field.
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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

TLS Online TPP Program

#Question id: 639

#Unit 1. Molecules and their Interaction Relevant to Biology

Match the coenzymes in column I enzymes to class of enzymes in column II

EnzymeReaction Type
A. Phosphofructokinase1. Redox reaction
B. Enolase2. Phosphoryl shift
C. Phosphoglycerate mutase3. Dehydration
D. Glyceraldehyde 3 Phosphate dehydrogenase4. Phosphoryl transfer