Tag: enzyme properties
Questions Related to enzyme properties
The enzymes are functional at
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0-5$^{\circ}$C
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15-25$^{\circ}$C
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25-40$^{\circ}$C
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70-85$^{\circ}$C
Enzymes works precisely at certain narrowly optimum conditions, such as appropriate temperature, pH, and ion concentration. Deviation from the optimal conditions adversely affects enzyme activity. Most enzymes have an optimal temperature, at which the rate of reaction is fastest. For human enzymes, the temperature optima are near the human body temperature (35-40$^o$C). Enzymatic reactions occur slowly or not at all at low temperatures. As the temperature increases, molecular motion increases, resulting in more molecular collisions. The rates of most enzyme-controlled reactions, therefore, increase as the temperature increases, within limits. High temperatures rapidly denature most enzymes. The molecular conformation (3-D shape) of the protein becomes altered as the hydrogen bonds responsible for its secondary, tertiary, and quaternary structures are broken. Because this inactivation is usually not reversible, activity is not regained when the enzyme is cooled.
Identify the incorrect statement about enzymes.
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They consist of proteins, with or without a non-protein part.
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They change the rate of the catalyzed reaction.
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They change the value of $\triangle$G of the reaction.
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They are not sensitive to heat.
Enzymes are biological catalyst which catalyze biological reactions. Most of the enzymes are proteins in nature. Some of the enzymes have non protein part which helps them to carry out reaction. Enzymes change the rate of chemical reaction by bringing about a decrease in free energy requirement. Thus, changing the free energy of the reaction. Because enzymes are proteins, they are highly sensitive to heat. Thus, enzymes catalyze reactions only at physiological conditions of temperature and pH.
In a chemical reaction, the
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Rate depends on the value of $\triangle$G.
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Rate depends on the activation energy.
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Entropy change depends in the activation energy.
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Activation energy depends on the value of $\triangle$G.
Which of the following is the transition state structure of the substrate formed during an enzymatic reaction?
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Permanent but unstable
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Transient and unstable
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Permanent and stable
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Transient but stable
Reactions do not undergo chemical changes automatically. They do so in transition states. Transition state has more free energy than reactants or products. Higher free energy helps in collision of transition state reactants. The enzymes binds to substrate molecules and form an unstable transient state called as transition state. The transition state rapidly undergoes degeneration into products and unchanged enzyme molecule.
In presence of an enzyme, the activation energy
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Increases
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Decreases
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First increases and then decreases
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Activation energy in not affected at all
As the water evaporates from the skin of a swimmer who has just left a pool, the swimmer begins to shiver and goose bumps form on his skin. As the blood vessels under his skin move more internally, the goose bumps that form and the shivering are reactions to counteract the lowering of body temperature. After the swimmer has dried off the shivering stops and his body temperature returns to normal. This is an example of
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Product inhibition
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Disequilibrium
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A negative feedback mechanism
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A positive feedback mechanism
When there is a drop in body temperature due to a drop in environmental temperature. The sensory receptors on the skin sends signal to the hypothalamus, which increases the body temperature by causing vasoconstriction and prevents blood from flowing closer to the skin, this also causes piloerection or goosebumps, this is to conserve energy and raise the body temperature. Once the swimmer has dried himself the thermosensors of the skin send a feed back of temperature returning to normal to the hypothalamus and the shivering is stopped. This is called negative feedback mechanism.
Who discovered the coenzymes?
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James Sumner
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Fritz Lipmann
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Mayerhoff
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Eduard Buchner
- Coenzymes are small organic molecules that can be loosely or tightly bound to an enzyme.
- Tightly bound coenzymes can be called as prosthetic groups. Coenzymes were discovered by Fritz Lipmann.
- His work on the coenzyme was awarded Nobel Prize in Physiology or Medicine, in 1953, for his discovery of coenzyme A and its importance for intermediary metabolism.
Hence, option B is the answer.
What is true for an enzyme during a biochemical reaction?
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It becomes part of the product
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It is unchanged
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It is broken down into amino acids
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It reacts with fatty acids
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It becomes a polypeptide
Any chemical reaction includes the formation of transition state between reactant and product. The energy required for formation of the transition state is termed as activation energy. Enzymes enhance the rate of reaction by lowering down the activation energy of transition state but themselves remain unchanged. Thus, the correct answer is option B.
Which of the following is iron porphyrin coenzyme or cofactor?
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Cytochrome
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FAD
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CoA
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NAD
Hemes are the iron containing porphyrins. They are extensively found in nature. These are also present in proteins like haemoglobin and myoglobin. Cytochromes are also a haemoproteins. Cytochrome also act as an integral part of membrane protein.
Biocatalysts were found accidently in Yeast extract by
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Sumner
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Kuhne
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Buchner
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Pasteur
Biocatalysts were found accidentally in yeast extract by Buchner in 1897. He prepared a yeast extract and added sugar solution to it. After sometime he noticed the alcohol formation in the extract which was a sign of fermentation which took in presence of enzyme. Later on, Sumner crystallized an enzyme known as urease and reported that all enzymes are protein.