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How many substrate molecules does a typical enzyme act on per second?
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∙ 10y ago
A single enzyme molecule can act on about 1000 substrate molecules per second.
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∙ 10y ago
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4 molecules of an enzyme and 60000 molecules of substrate are taken all substrate molecules are converted into products in 5 minutes calculate turnover number of enzyme?
Assuming that the turnover number is 5000 per second, which you did not specify, than the number of molecules that can be reached by the enzyme in 5 minutes is just this:5 minutes * 60 seconds/minute * 5000 turnover/second = 150,000 turnoversThis is because 1 turnover counts as one molecule reached by the enzyme.If instead the turnover number was 5000 per minute, then it would be:5 minutes * 5000 turnovers/minute = 25,000 turnovers.If it was 5000 per hour, then it would be:5 minutes * 1 hour/60 minutes * 5000 turnovers/hour = 416.7 turnovers.
What are the 3 factors that can change the rate of enzyme reaction?
The first factor is Enzyme concentration or subtrate concentration.The rate of enzyme action is directly proportional to to the availability of enzyme provided the substrate concentration unlimited.Or the rate is directly proportional to the substrate concentration if enzymes are limited but if enzyme concentration is kept constant then upto the certain level the increase in substrate amount will no longer increase the rate of enzyme action. Second factor is temperature.The rate if an enzyme action is always directly proportional to the increase in temperature but upto the specific limit called as optimum temperature. Third factor is the pH value.Enzymes can work efficiently over a narrow range of pH called as Optimum pH.A minor change in pH value can denature the enzyme.
What effect does an increase in pH have on enzyme reaction?
It will very likely change it in some way. It's impossible to be more specific without knowing what enzyme and what pH.From the optimum conditions, an increase in pH will increase the number of OH- ions, and these will affect the charge of areas on the tertiary structure of the protein (remember that enzymes are proteins). This will cause a conformational (shape) change in the protein (enzyme), and therefore denatures it, as the active site is no longer complimentary to the substrate. This will lead to fewer Enzyme-Substrate complexes per second when using a lot of enzymes, and will decrease the rate of the enzyme reaction.
In glycolysis ATP molecules are produced by .?
In glycolysis, ATP molecules are produced by? a- oxidative phosphorylation b-substrate-level phosphorylation c-cellular respiration d-photophosphorylation e-photosynthesis
What is the fastest enzyme in body?
Catalase is. it is an enzyme located in the liver that breaks down poisonous hydrogen peroxide into water and oxygen ( 2 H2O2 -----> 2 H2O + O2) and it is estimated to catalyse around 38 million molecules of hydrogen peroxide per second!
What should be done in order to keep the rate constant over the entire time course?
add more substrate. The rate of the reaction drops when the enzyme no longer has a maximum number of substrate molecules to interact with. Above the maximum substrate concentration, the rate will not be increased by adding more substrate; the enzyme is already working as fast as it can. An enzyme can catalyze a certain number of reactions per second, and if there is not sufficient substrate present for it to work at its maximum velocity, the rate will decrease. Therefore, to keep the enzyme working at its maximum, you must add more substrate.
How fast do enzymes act?
Enzymes reaction cycle is so fast that a single enzyme molecule typically act on about thousand substrate molecules per second.
Where is the substrate that binds to an enzyme?
A substrate molecule needs to interact with the enzyme's active center (known as "active site") for the enzyme mediated catalytic conversion of substrate into product. Some times, this could or may bind to a second site of an enzyme named, "allosteric site" that would not form the product.
What is the advantage of enzymes not being used up in reactions?
Let say enzyme 1 has a shape of A. When it encounters a solute particle of shape A', enzyme jumps on the particle so to speak changing its shape to A'' and back to A' in less than nano second and when that shape change happens the solute particle becomes highly unstable and now can react with other solute particles and hence carry out the reaction. Enzyme jumps on substrate --> substrate unstable --> enzyme jumps back out of substrate --> unstable substrate reacts with another substrate.
4 molecules of an enzyme and 60000 molecules of substrate are taken all substrate molecules are converted into products in 5 minutes calculate turnover number of enzyme?
Assuming that the turnover number is 5000 per second, which you did not specify, than the number of molecules that can be reached by the enzyme in 5 minutes is just this:5 minutes * 60 seconds/minute * 5000 turnover/second = 150,000 turnoversThis is because 1 turnover counts as one molecule reached by the enzyme.If instead the turnover number was 5000 per minute, then it would be:5 minutes * 5000 turnovers/minute = 25,000 turnovers.If it was 5000 per hour, then it would be:5 minutes * 1 hour/60 minutes * 5000 turnovers/hour = 416.7 turnovers.
How can you describe the enzyme-substrate complex?
Enzyme-substrate complex (or ES complex) is the key to understand the kinetic behavior of the enzymes. The ES complex represents just the starting point for the catalysis reaction.The kinetic pattern of enzymes was led by Victor Henri in 1903. He proposed that an enzyme combines with its substrate molecule to form the ES complex as a necessary step in enzyme catalysis. This idea expanded into a general theory of enzyme action, particularly by Leonor Michaelis and Maud Menten in 1913, who postulated that the enzyme (E) first combines reversibly with its substrate to form an enzyme-substrate complex (ES )in a relatively fast reversible step. The ES complex then breaks down in a slower second step to yield the free enzyme and a product (P), according to the following equation:E + S < > ES > E + P
What are the 3 factors that can change the rate of enzyme reaction?
The first factor is Enzyme concentration or subtrate concentration.The rate of enzyme action is directly proportional to to the availability of enzyme provided the substrate concentration unlimited.Or the rate is directly proportional to the substrate concentration if enzymes are limited but if enzyme concentration is kept constant then upto the certain level the increase in substrate amount will no longer increase the rate of enzyme action. Second factor is temperature.The rate if an enzyme action is always directly proportional to the increase in temperature but upto the specific limit called as optimum temperature. Third factor is the pH value.Enzymes can work efficiently over a narrow range of pH called as Optimum pH.A minor change in pH value can denature the enzyme.
What enzyme can convert 40 million molecules of hydrogen peroxide to harmless water and oxygen every second?
Catalase
Can enzymes become saturated?
It takes time (although usually a very small amount) for an enzyme molecule to catalyze a reaction. An enzyme solution is said to be saturated if all the molecules of enzyme in the solution are operating at full capacity (all active sites binding substrate molecules). Some enzymes are easily saturated (RuBisCo - 3 reactions/second) due to the highly energetically-demanding reactions that they catalyze while other enzymes that catalyze relatively simple reactions (amylase - many many reactions/second) are harder to saturate.
What effect does an increase in pH have on enzyme reaction?
It will very likely change it in some way. It's impossible to be more specific without knowing what enzyme and what pH.From the optimum conditions, an increase in pH will increase the number of OH- ions, and these will affect the charge of areas on the tertiary structure of the protein (remember that enzymes are proteins). This will cause a conformational (shape) change in the protein (enzyme), and therefore denatures it, as the active site is no longer complimentary to the substrate. This will lead to fewer Enzyme-Substrate complexes per second when using a lot of enzymes, and will decrease the rate of the enzyme reaction.
What makes enzymes speed up the chemical rate?
The ability to attract similar molecules that bond, whereas without the enzyme, the molecules would have to hit in a same position at the exact molecule needed for bonding. An enzyme is able to do this many times in a second, thus speeding up the reaction.
In glycolysis ATP molecules are produced by .?
In glycolysis, ATP molecules are produced by? a- oxidative phosphorylation b-substrate-level phosphorylation c-cellular respiration d-photophosphorylation e-photosynthesis
