What is the substrate for aldolase reaction?

What is the substrate for aldolase reaction?
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Fructose-1,6-bisphosphate.
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A substrate for the enzyme aldolase is (A) galactose-6-phosphate (B) isocitric acid (C) Glucose-1-phosphate (D) Fructose 1, 6 diphosphate

Description : A substrate for the enzyme aldolase is (A) galactose-6-phosphate (B) isocitric acid (C) Glucose-1-phosphate (D) Fructose 1, 6 diphosphate

Last Answer : Answer : D

Which of the following is a substrate for aldolase activity in Glycolytic pathway? (A) Glyceraldehyde-3-p (B) Glucose-6-p (C) Fructose-6-p (D) Fructose1, 6-bisphosphate

Description : Which of the following is a substrate for aldolase activity in Glycolytic pathway? (A) Glyceraldehyde-3-p (B) Glucose-6-p (C) Fructose-6-p (D) Fructose1, 6-bisphosphate

Last Answer : D

Conversion of glucose to glucose-6-phosphate, the first irreversible reaction of glycolysis, is catalysed by (a) phosphofructokinase (b) aldolase (c) hexokinase (d) enolase.

Description : Conversion of glucose to glucose-6-phosphate, the first irreversible reaction of glycolysis, is catalysed by (a) phosphofructokinase (b) aldolase (c) hexokinase (d) enolase.

Last Answer : (c) hexokinase

Zinc is a constituent of the enzyme: (A) Succinate dehydrogenase (B) Carbonic anhydrase (C) Mitochondrial superoxide dismutase (D) Aldolase

Description : Zinc is a constituent of the enzyme: (A) Succinate dehydrogenase (B) Carbonic anhydrase (C) Mitochondrial superoxide dismutase (D) Aldolase

Last Answer : Answer : B

A mitochondrial marker enzyme is (A) Aldolase (B) Amylase (C) Succinic dehydrogenase (D) Pyruvate dehydrogenase ENZYMES 175

Description : A mitochondrial marker enzyme is (A) Aldolase (B) Amylase (C) Succinic dehydrogenase (D) Pyruvate dehydrogenase ENZYMES 175

Last Answer : Answer : C

Essential fructosuria is characterized by the lack of the hepatic enzyme: (A) Phosphohexose isomerase (B) Aldalose A (C) Aldolase B (D) Fructokinase

Description : Essential fructosuria is characterized by the lack of the hepatic enzyme: (A) Phosphohexose isomerase (B) Aldalose A (C) Aldolase B (D) Fructokinase

Last Answer : Answer : D

Hemolytic anemia is caused by the deficiency of certain enzymes of the pentose phosphate pathway, the principal enzyme involved is (A) Glucose-6-phosphate dehydrogenase (B) Aldolase (C) Fructose 1, 6-bisphosphatase (D) Phosphohexose isomerase

Description : Hemolytic anemia is caused by the deficiency of certain enzymes of the pentose phosphate pathway, the principal enzyme involved is (A) Glucose-6-phosphate dehydrogenase (B) Aldolase (C) Fructose 1, 6-bisphosphatase (D) Phosphohexose isomerase

Last Answer : Answer : A

The enzyme of the glycolic pathway, sensitive to inhibiton by fluoride ions is (A) Hexokinase (B) Aldolase (C) Enolase (D) Pyruvate kinase

Description : The enzyme of the glycolic pathway, sensitive to inhibiton by fluoride ions is (A) Hexokinase (B) Aldolase (C) Enolase (D) Pyruvate kinase

Last Answer : Answer : C

Enzyme involved in joining together two substrates is (A) Glutamine synthetase (B) Aldolase (C) Gunaine deaminase (D) Arginase

Description : Enzyme involved in joining together two substrates is (A) Glutamine synthetase (B) Aldolase (C) Gunaine deaminase (D) Arginase

Last Answer : Answer : A

An example of ligases is (A) Succinate thiokinase (B) Alanine racemase (C) Fumarase (D) Aldolase

Description : An example of ligases is (A) Succinate thiokinase (B) Alanine racemase (C) Fumarase (D) Aldolase

Last Answer : Answer : A

The following enzyme is required for the hexose monophosphate shunt pathway: (A) Glucose-6-phosphatase (B) Phosphorylase (C) Aldolase (D) Glucose-6-phosphate dehydrogenase

Description : The following enzyme is required for the hexose monophosphate shunt pathway: (A) Glucose-6-phosphatase (B) Phosphorylase (C) Aldolase (D) Glucose-6-phosphate dehydrogenase

Last Answer : D

During glycolysis, Fructose 1, 6 diphosphate is decomposed by the enzyme: (A) Enolase a (B) Fructokinase (C) Aldolase (D) Diphosphofructophosphatose

Description : During glycolysis, Fructose 1, 6 diphosphate is decomposed by the enzyme: (A) Enolase a (B) Fructokinase (C) Aldolase (D) Diphosphofructophosphatose

Last Answer : C

Feedback term refers to (A) Effect of substrate on rate of enzymatic reaction (B) Effect of end product on rate reaction (C) Effect of enzyme concentration on rate of reaction (D) Effect of external compound on rate of reaction

Description : Feedback term refers to (A) Effect of substrate on rate of enzymatic reaction (B) Effect of end product on rate reaction (C) Effect of enzyme concentration on rate of reaction (D) Effect of external compound on rate of reaction

Last Answer : Answer : B

Template/lock and key theory of enzyme action is supported by (A) Enzymes speed up reaction (B) Enzymes occur in living beings and speed up certain reactions (C) Enzymes determine the direction of reaction (D) Compounds similar to substrate inhibit enzyme activity

Description : Template/lock and key theory of enzyme action is supported by (A) Enzymes speed up reaction (B) Enzymes occur in living beings and speed up certain reactions (C) Enzymes determine the direction of reaction (D) Compounds similar to substrate inhibit enzyme activity

Last Answer : Answer : D

An enzyme promotes a chemical reaction by (A) Lowering the energy of activation (B) Causing the release of heat which acts as a primer (C) Increasing molecular motion (D) Changing the free energy difference between substrate and product

Description : An enzyme promotes a chemical reaction by (A) Lowering the energy of activation (B) Causing the release of heat which acts as a primer (C) Increasing molecular motion (D) Changing the free energy difference between substrate and product

Last Answer : Answer : A

The rate of an enzyme catalyzed reaction was measured using several substrate concentrations that were much lower than Km, the dependence of reaction velocity on substrate concentration can best be described as (A) Independent of enzyme concentration (B) A constant fraction of Vmax (C) Equal to Km (D) Proportional to the substrate concentration

Description : The rate of an enzyme catalyzed reaction was measured using several substrate concentrations that were much lower than Km, the dependence of reaction velocity on substrate concentration can best be ... constant fraction of Vmax (C) Equal to Km (D) Proportional to the substrate concentration

Last Answer : Answer : C

When [s] is equal to Km, which of the following conditions exist? (A) Half the enzyme molecules are bound to substrate (B) The velocity of the reaction is equal to Vmax (C) The velocity of the reaction is independent of substrate concentration (D) Enzyme is completely saturated with substrate

Description : When [s] is equal to Km, which of the following conditions exist? (A) Half the enzyme molecules are bound to substrate (B) The velocity of the reaction is equal to Vmax (C) The velocity of the reaction is independent of substrate concentration (D) Enzyme is completely saturated with substrate

Last Answer : Answer : A

The Michaehis-Menten hypothesis: (A) Postulates the formation of an enzyme substrate complex (B) Enables us to calculate the isoelectric point of an enzyme (C) States that the rate of a chemical reaction may be independent of substrate concentration (D) States that the reaction rate is proportional to substrate concentration

Description : The Michaehis-Menten hypothesis: (A) Postulates the formation of an enzyme substrate complex (B) Enables us to calculate the isoelectric point of an enzyme (C) States that the ... independent of substrate concentration (D) States that the reaction rate is proportional to substrate concentration

Last Answer : Answer : A

If a coenzyme is required in an enzyme reaction, the former usually has the function of (A) Acting as an acceptor for one of the cleavage products of the substrate (B) Enhancing the specificity of the apo enzyme (C) Increasing the number of receptor sites of the apo enzyme (D) Activating the substrate ENZYMES 167

Description : If a coenzyme is required in an enzyme reaction, the former usually has the function of (A) Acting as an acceptor for one of the cleavage products of the substrate (B) Enhancing the specificity ... C) Increasing the number of receptor sites of the apo enzyme (D) Activating the substrate ENZYMES 167

Last Answer : Answer : A

If the substrate concentration is much below the km of the enzyme, the velocity of the reaction is (A) Directly proportional to substrate concentration (B) Not affected by enzyme concentration (C) Nearly equal to Vmax (D) Inversely proportional to substrate concentration

Description : If the substrate concentration is much below the km of the enzyme, the velocity of the reaction is (A) Directly proportional to substrate concentration (B) Not affected by enzyme concentration (C) Nearly equal to Vmax (D) Inversely proportional to substrate concentration

Last Answer : Answer : A

When the velocity of an enzymatic reaction equals Vmax, substrate concentration is (A) Half of Km (B) Equal to Km (C) Twice the Km (D) Far above the Km

Description : When the velocity of an enzymatic reaction equals Vmax, substrate concentration is (A) Half of Km (B) Equal to Km (C) Twice the Km (D) Far above the Km

Last Answer : Answer : D

An allosteric enzyme is generally inhibited by (A) Initial substrate of the pathway (B) Substrate analogues (C) Product of the reaction catalysed by allosteric enzyme (D) Product of the pathway

Description : An allosteric enzyme is generally inhibited by (A) Initial substrate of the pathway (B) Substrate analogues (C) Product of the reaction catalysed by allosteric enzyme (D) Product of the pathway

Last Answer : Answer : D

Example of enzyme specificity: (A) Stereo specificity (B) Reaction specificity (C) Substrate specificity(D) All of these

Description : Example of enzyme specificity: (A) Stereo specificity (B) Reaction specificity (C) Substrate specificity(D) All of these

Last Answer : Answer : D

The example of generation of a high energy phosphate at the substrate level in the citric acid cycle is the reaction: (A) Isocitrate α-Ketoglutarate (B) Succinate α-fumarate (C) Malate α-oxaloacetate (D) Succinyl CoA α-Succinate

Description : The example of generation of a high energy phosphate at the substrate level in the citric acid cycle is the reaction: (A) Isocitrate α-Ketoglutarate (B) Succinate α-fumarate (C) Malate α-oxaloacetate (D) Succinyl CoA α-Succinate

Last Answer : Answer : D

A sigmoidal plot of substrate concentration ([S]) verses reaction velocity (V) may indicate (A) Michaelis-Menten kinetics (B) Co-operative binding (C) Competitive inhibition (D) Non-competitive inhibition

Description : A sigmoidal plot of substrate concentration ([S]) verses reaction velocity (V) may indicate (A) Michaelis-Menten kinetics (B) Co-operative binding (C) Competitive inhibition (D) Non-competitive inhibition

Last Answer : Answer : B

From the L ineweaver-Burk p lot of Michaelis-Menten equation, Km and Vmax can be determined when V is the reaction velocity at substrate concentration S, the X-axis experimental data are expressed as (A) 1/V (B) V (C) 1/S (D) S

Description : From the L ineweaver-Burk p lot of Michaelis-Menten equation, Km and Vmax can be determined when V is the reaction velocity at substrate concentration S, the X-axis experimental data are expressed as (A) 1/V (B) V (C) 1/S (D) S

Last Answer : Answer : C

Isoenzymes for a given reaction (A) Have different spedificities (B) Have identical affinities for the same substrate (C) Exhibit different electrophoretic motilities (D) Contain similar ratios of different polypeptide chains

Description : Isoenzymes for a given reaction (A) Have different spedificities (B) Have identical affinities for the same substrate (C) Exhibit different electrophoretic motilities (D) Contain similar ratios of different polypeptide chains

Last Answer : Answer : B

The reaction catalysed by phosphofructokinase (A) Is activated by high concentrations of ATP and citrate (B) Uses fruitose-1-phosphate as substrate (C) Is the rate-limiting reaction of the glycolytic pathway (D) Is inhibited by fructose 2, 6-bisphosphate

Description : The reaction catalysed by phosphofructokinase (A) Is activated by high concentrations of ATP and citrate (B) Uses fruitose-1-phosphate as substrate (C) Is the rate-limiting reaction of the glycolytic pathway (D) Is inhibited by fructose 2, 6-bisphosphate

Last Answer : C

Out of 24 mols of ATP formed in TCA cycle, 2 molecules of ATP can be formed at “substrate level” by which of the following reaction ? (A) Citric acid→ Isocitric acid (B) Isocitrate→ Oxaloacetate (C) Succinic acid→ Fumarate (D) Succinylcat→ Succinic acid

Description : Out of 24 mols of ATP formed in TCA cycle, 2 molecules of ATP can be formed at “substrate level” by which of the following reaction ? (A) Citric acid→ Isocitric acid (B) Isocitrate→ Oxaloacetate (C) Succinic acid→ Fumarate (D) Succinylcat→ Succinic acid

Last Answer : D

Aldolase test?

Description : Aldolase test?

Last Answer : DefinitionAldolase is a protein (called an enzyme) that helps break down certain sugars into energy. It is found in high amounts in muscle tissue.A test can be done to measure the amount of aldolase ... .Once the blood has been collected, the needle is removed, and the puncture site is covered to

Regulator gene controls chemical synthesis (Operon concept) by (a) Inhibiting transcription of mRNA (b) Inhibiting enzymes (c) Inhibiting passage of mRNA (d) Inhibiting substrate enzyme reaction

Description : Regulator gene controls chemical synthesis (Operon concept) by (a) Inhibiting transcription of mRNA (b) Inhibiting enzymes (c) Inhibiting passage of mRNA (d) Inhibiting substrate enzyme reaction

Last Answer : Ans. ((a))

Transition state structure of the substrate formed during an enzymatic reaction is (a) transient and unstable (b) permanent and stable (c) transient but stable (d) permanent but unstable.

Description : Transition state structure of the substrate formed during an enzymatic reaction is (a) transient and unstable (b) permanent and stable (c) transient but stable (d) permanent but unstable.

Last Answer : (a) transient and unstable

Which of the following describes the given graph correctly? Potential energy Reaction Product Substrate B A (a) Endothermic reaction with energy A in presence of enzyme and B in absence of enzyme. (b) Exothermic reaction with energy A in presence of enzyme and B in absence of enzyme. (c) Endothermic reaction with energy A in absence of enzyme and B in presence of enzyme. (d) Exothermic reaction with energy A in absence of enzyme and B in presence of enzyme.

Description : Which of the following describes the given graph correctly? Potential energy Reaction Product Substrate B A (a) Endothermic reaction with energy A in presence of enzyme and B in absence of enzyme. (b) ... . (d) Exothermic reaction with energy A in absence of enzyme and B in presence of enzyme.

Last Answer : (b) Exothermic reaction with energy A in presence of enzyme and B in absence of enzyme

Oxidative phosphorylation involves (A) Electron transport system (B) Substrate level phosphorylation (C) Reaction catalyzed by succinic thiokinase in TCA cycle (D) None of the above

Description : Oxidative phosphorylation involves (A) Electron transport system (B) Substrate level phosphorylation (C) Reaction catalyzed by succinic thiokinase in TCA cycle (D) None of the above

Last Answer : (A) Electron transport system

A common substrate of HGPRTase, APRTase and PRPP glutamyl amidotransferase is (A) Ribose 5 phosphate (B) Phosphoribosyl pyrophosphate (C) Hypoxanthine (D) Adenosine

Description : A common substrate of HGPRTase, APRTase and PRPP glutamyl amidotransferase is (A) Ribose 5 phosphate (B) Phosphoribosyl pyrophosphate (C) Hypoxanthine (D) Adenosine

Last Answer : Answer : B

An alternate substrate for orotate phosphoribosyl transferase is (A) Allopurinol (B) Xanthine (C) Hypoxanthine (D) Adenine

Description : An alternate substrate for orotate phosphoribosyl transferase is (A) Allopurinol (B) Xanthine (C) Hypoxanthine (D) Adenine

Last Answer : Answer : D

A substrate for enzymes of pyrimidine nucleotide biosynthesis is (A) Allopurinol (B) Tetracylin (C) Chloramphenicol (D) Puromycin

Description : A substrate for enzymes of pyrimidine nucleotide biosynthesis is (A) Allopurinol (B) Tetracylin (C) Chloramphenicol (D) Puromycin

Last Answer : Answer : A

Substrate-linked phosphorylation occurs in (A) Glycolytic pathway(B) Citric acid cycle (C) Both (A) and (B) (D) None of these

Description : Substrate-linked phosphorylation occurs in (A) Glycolytic pathway(B) Citric acid cycle (C) Both (A) and (B) (D) None of these

Last Answer : Answer : C

Substrate concentration at which an enzyme attains half its maximum velocity is (A) Threshold value (B) Michaelis-Menton constant (C) Concentration level (D) None of these

Description : Substrate concentration at which an enzyme attains half its maximum velocity is (A) Threshold value (B) Michaelis-Menton constant (C) Concentration level (D) None of these

Last Answer : Answer : B

Km value of enzyme is substrate concentration at (A) ½ Vmax (B) 2 Vmax (C) ½ Vmax (D) 4 Vmax

Description : Km value of enzyme is substrate concentration at (A) ½ Vmax (B) 2 Vmax (C) ½ Vmax (D) 4 Vmax

Last Answer : Answer : D

The ratio of enzyme to substrate molecules can be as low as (A) 1 : 100,000 (B) 1 : 500,000 (C) 1 : 10,000 (D) 1 : 1,000

Description : The ratio of enzyme to substrate molecules can be as low as (A) 1 : 100,000 (B) 1 : 500,000 (C) 1 : 10,000 (D) 1 : 1,000

Last Answer : Answer : A

Allosteric inhibition (A) Makes active site unifit for substrate (B) Controls excess formation and end product (C) Both (A) and (B) (D) None of these

Description : Allosteric inhibition (A) Makes active site unifit for substrate (B) Controls excess formation and end product (C) Both (A) and (B) (D) None of these

Last Answer : Answer : C

Feedback inhibition of enzyme is influenced by (A) Enzyme (B) External factors (C) End product (D) Substrate

Description : Feedback inhibition of enzyme is influenced by (A) Enzyme (B) External factors (C) End product (D) Substrate

Last Answer : Answer : C

Enzyme inhibition caused by a substance resembling substrate molecule is (A) Competitive inhibition (B) Non-competitive inhibition (C) Feedback inhibition (D) Allosteric inhibition

Description : Enzyme inhibition caused by a substance resembling substrate molecule is (A) Competitive inhibition (B) Non-competitive inhibition (C) Feedback inhibition (D) Allosteric inhibition

Last Answer : Answer : A

Combination of apoenzyme and coenzyme produces (A) Prosthetic group (B) Holoenzyme (C) Enzyme substrate complex (D) Enzyme product complex

Description : Combination of apoenzyme and coenzyme produces (A) Prosthetic group (B) Holoenzyme (C) Enzyme substrate complex (D) Enzyme product complex

Last Answer : Answer : B

Feedback inhibition of enzyme action is affected by (A) Enzyme (B) Substrate (C) End products (D) None of these

Description : Feedback inhibition of enzyme action is affected by (A) Enzyme (B) Substrate (C) End products (D) None of these

Last Answer : Answer : C

The shape of an enzyme and consequently its activity can be reversibly altered from moment to moment by (A) Heat (B) Amino acid substrate (C) Allosteric subunits (D) Sulfur substitutions

Description : The shape of an enzyme and consequently its activity can be reversibly altered from moment to moment by (A) Heat (B) Amino acid substrate (C) Allosteric subunits (D) Sulfur substitutions

Last Answer : Answer : C

Which one of the following statements is not characteristic of allosteric enzymes? (A) They frequently catalyze a committed step early in a metabolic pathway (B) They are often composed of subunits (C) They follow Michaelis-Menten kinetics (D) They frequently show cooperativity for substrate binding

Description : Which one of the following statements is not characteristic of allosteric enzymes? (A) They frequently catalyze a committed step early in a metabolic pathway (B) They are often composed of subunits (C) They follow Michaelis-Menten kinetics (D) They frequently show cooperativity for substrate binding

Last Answer : Answer : C

The Michaelis constant, Km is (A) Numerically equal to ½ Vmax (B) Dependent on the enzyme concentration (C) Independent of pH (D) Numerically equal to the substrate concentration that gives half maximal velocity

Description : The Michaelis constant, Km is (A) Numerically equal to ½ Vmax (B) Dependent on the enzyme concentration (C) Independent of pH (D) Numerically equal to the substrate concentration that gives half maximal velocity

Last Answer : Answer : D