Name the most common substrate used for respiration. -Biology

Name the most common substrate used for respiration. -Biology
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Which one of the following is the correct mathcing of the site of action on the given substrate, the enzyme acting upon it and the end producrt?

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Last Answer : The substrate for photorespiration is A. Glycolate B. Glucose C. Pyruvic acid D. Acetyl CoA

The substrate for photorespiration is

Description : The substrate for photorespiration is

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The substrate for photorespiration is

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Explain the process of digestion if a student puts a plain cracker in their mouth, chews it, and holds the mush in their mouth. Mention the pH, temperature, enzyme, substrate and products. ?

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

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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

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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

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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

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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

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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

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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

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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

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

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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

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

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

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 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 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

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

Enzymes activity is controlled by (A) pH of the solution (B) Temperature (C) Concentration of the enzyme (D) Concentration of the substrate (E) All of these

Description : Enzymes activity is controlled by (A) pH of the solution (B) Temperature (C) Concentration of the enzyme (D) Concentration of the substrate (E) All of these

Last Answer : Answer : C

‘Lock’ and ‘Key’ model of enzyme action proposed by Fisher implies that (A) The active site is flexible and adjusts to substrate (B) The active site requires removal of PO4 group (C) The active site is complementary in shape to that of the substrate (D) Substrates change conformation prior to active site interaction

Description : Lock' and Key' model of enzyme action proposed by Fisher implies that (A) The active site is flexible and adjusts to substrate (B) The active site requires removal of PO4 group ( ... complementary in shape to that of the substrate (D) Substrates change conformation prior to active site interaction

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

A competitive inhibitor of an enzyme has which of the following properties? (A) It is frequently a feedback inhibitor (B) It becomes covalently attached to an enzyme (C) It decreases the Vmax (D) It interferes with substrate binding to the enzyme

Description : A competitive inhibitor of an enzyme has which of the following properties? (A) It is frequently a feedback inhibitor (B) It becomes covalently attached to an enzyme (C) It decreases the Vmax (D) It interferes with substrate binding to the enzyme

Last Answer : Answer : D

An allosteric enzyme influences the enzyme activity by (A) Competiting for the catalytic site with the substrate (B) Changing the specificity of the enzyme for the substrate (C) Changing the conformation of the enzyme by binding to a site other than catalytic site (D) Changing the nature of the products formed

Description : An allosteric enzyme influences the enzyme activity by (A) Competiting for the catalytic site with the substrate (B) Changing the specificity of the enzyme for the substrate (C) Changing the conformation ... binding to a site other than catalytic site (D) Changing the nature of the products formed

Last Answer : Answer : C

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

Velocity maximum for an enzyme at half the substrate concentration gives (A) The molecular weight of the enzyme (B) Km value (C) Isoelectric pH (D) Pk value

Description : Velocity maximum for an enzyme at half the substrate concentration gives (A) The molecular weight of the enzyme (B) Km value (C) Isoelectric pH (D) Pk value

Last Answer : Answer : B

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