Proto-oncogenes can change into oncogenes that cause cancer. Which of the following best explains the presence of these potential time bombs in eukaryotic cells?

#Question id: 10284

#I Life Science/ Life Sciences Group – I-V

Allosteric regulation of enzyme multisubunit or multiactive site shows cooperativity with the sigmoidal graph between substerate conc. v/s Activity,

a) Cell contain NADH, FADH2 and ATP, that inhibits the allosteric enzyme activity by lowering the affinity with its substate, graph shifts towards B from control

 b) A- shows low ATP, the Km for fructose 6-phosphate is relatively low, the affinity of the enzyme with its substate is relatively high

 c) Haemoglobin, Phosphofructokinase, Phosphate dehydrogenase complex, α-ketoglutarate dehydrogenase complex, these all enzymes shows characteristics of sigmoidal graph

 d) When ATP is high, Km for fructose 6-phosphate is greatly increased- this activity shown by B in the graph

 e) fructose 2,6-bisphosphate binds to its allosteric site on PFK-1, it increases the enzyme’s affinity for its substrate fructose 6-phosphate and reduces its affinity for the allosteric inhibitors ATP and citrate- shown in graph by A

 Which of the following  combination of the enzyme activity with its substate correctly shown;

#Question id: 10284

#SCPH05 I Biotechnology

Allosteric regulation of enzyme multisubunit or multiactive site shows cooperativity with the sigmoidal graph between substerate conc. v/s Activity,

a) Cell contain NADH, FADH2 and ATP, that inhibits the allosteric enzyme activity by lowering the affinity with its substate, graph shifts towards B from control

 b) A- shows low ATP, the Km for fructose 6-phosphate is relatively low, the affinity of the enzyme with its substate is relatively high

 c) Haemoglobin, Phosphofructokinase, Phosphate dehydrogenase complex, α-ketoglutarate dehydrogenase complex, these all enzymes shows characteristics of sigmoidal graph

 d) When ATP is high, Km for fructose 6-phosphate is greatly increased- this activity shown by B in the graph

 e) fructose 2,6-bisphosphate binds to its allosteric site on PFK-1, it increases the enzyme’s affinity for its substrate fructose 6-phosphate and reduces its affinity for the allosteric inhibitors ATP and citrate- shown in graph by A

 Which of the following  combination of the enzyme activity with its substate correctly shown;

#Question id: 10285

#I Life Science/ Life Sciences Group – I-V

Some of the statements given shows the activity of PFK-1 and PFK-2, which of the following statements incorrectly shown these enzyme activity?

#Question id: 10285

#SCPH05 I Biotechnology

Some of the statements given shows the activity of PFK-1 and PFK-2, which of the following statements incorrectly shown these enzyme activity?

#Question id: 10286

#I Life Science/ Life Sciences Group – I-V

The enzyme aldolase, catalyzes a reversible aldol condensation, Fructose 1,6-bisphosphate is cleaved to yield two different triose phosphates, glyceraldehyde 3-phosphate, an aldose, and dihydroxyacetone phosphate, a ketose. There are two classes of aldolases such as;

A) Class I aldolases

B) Class II aldolases

i) Found in animals and plants

ii) Found in in fungi and bacteria

iii) formation of protonated Schiff base on enzyme and its active site contain lysine residue

iv) do not form the Schiff base intermediate and a zinc ion at the active site is coordinated with the carbonyl oxygen at C-2

In which of the following option is the given enzyme with its correct statements?

#Question id: 10286

#SCPH05 I Biotechnology

The enzyme aldolase, catalyzes a reversible aldol condensation, Fructose 1,6-bisphosphate is cleaved to yield two different triose phosphates, glyceraldehyde 3-phosphate, an aldose, and dihydroxyacetone phosphate, a ketose. There are two classes of aldolases such as;

A) Class I aldolases

B) Class II aldolases

i) Found in animals and plants

ii) Found in in fungi and bacteria

iii) formation of protonated Schiff base on enzyme and its active site contain lysine residue

iv) do not form the Schiff base intermediate and a zinc ion at the active site is coordinated with the carbonyl oxygen at C-2

In which of the following option is the given enzyme with its correct statements?