ANSWERTRIVIA.COM: We ask you, humbly: don't scroll away.

Dear Reader, If you use ANSWERTRIVIA a lot, this message is for you. We're sure you are busy so we'll make this quick: Today we need your help. We don't have salespeople. We depend on donations from exceptional readers, but fewer than 2% give. If you donate just a coffee, lunch or whatever you can today, ANSWERTRIVIA could keep thriving. Thank you.
(Secure PayPal)
*Everything counts! No minimum threshold!
Thank you for inspiring us!

Enter Another Question

4/16/21

[Answer] enzymes work by ________

Answer: reducing activation energy




Most relevant text from all around the web:


enzymes work by ________ Enzyme kinetics is the investigation of how enzymes bind substrates and turn them into products. The rate data used in kinetic analyses are commonly obtained from enzyme assays. In 1913 Leonor Michaelis and Maud Leonora Menten proposed a quantitative theory of enzyme kinetics which is referred to as Michaelis–Menten kinetics . The major contribution of Michaelis and Menten was to think of enzyme reactions in two stages. In the first the substrate binds reversibly to the enzyme forming the enzyme-substrate complex. This is sometimes called the Michaelis–Menten complex in their honor. Th… Enzyme kinetics is the investigation of how enzymes bind substrates and turn them into products. The rate data used in kinetic analyses are commonly obtained from enzyme assays. In 1913 Leonor Michaelis and Maud Leonora Menten proposed a quantitative theory of enzyme kinetics which is referred to as Michaelis–Menten kinetics. The major contribution of Michaelis and Menten was to think of enzyme reactions in two stages. In the first the substrate binds reversibly to the enzyme forming the enzyme-substrate complex. This is sometimes called the Michaelis–Menten complex in their honor. The enzyme then catalyzes the chemical step in the reaction and releases the product. This work was further developed by G. E. Briggs and J. B. S. Haldane who derived kinetic equations that are still widely used today. Enzyme rates depend on solution conditions and substrate concentration. To find the maximum speed of an enzymatic reaction the substrate concentration is increased until a constant rate of product formation is seen. This is shown in the saturation curve on the right. Saturation happens because as substrate concentration increases more and more of the free enzyme is converted into the substrate-bound ES complex. At the maximum reaction rate (Vmax) of the enzyme all the enzyme active sites are bound to substrate and the amount of ES complex is the same as the total amount of enzyme. Vmax is only one of several important kinetic parameters. The amount of substrate needed to achieve a given rate of reaction is also important. This is given by the Michaelis–Menten constant (Km) which is the substrate concentration required for an enzyme to reach one-half its maxim...


Disclaimer: 

Our tool is still learning and trying its best to find the correct answer to your question. Now its your turn, "The more we share The more we have". Comment any other details to improve the description, we will update answer while you visit us next time...Kindly check our comments section, Sometimes our tool may wrong but not our users.


Are We Wrong To Think We're Right? Then Give Right Answer Below As Comment

No comments:

Post a Comment